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- PDB-9e2g: Cryo-EM structure of 48 nm repeat of microtubule doublet from T. ... -

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Basic information

Entry
Database: PDB / ID: 9e2g
TitleCryo-EM structure of 48 nm repeat of microtubule doublet from T. brucei flagellum
Components
  • (Cilia- and flagella-associated protein ...) x 4
  • (EF-hand domain-containing ...) x 8
  • (Enkurin domain-containing ...) x 4
  • (Nucleoside diphosphate kinase, ...) x 2
  • (T. brucei spp.-specific ...) x 2
  • (Trichohyalin-plectin-homology domain-containing ...) x 2
  • CCDC81 HU domain-containing protein
  • CMF34/CARP4
  • Calcium-binding protein, putative
  • Calpain-like cysteine peptidase, putative
  • Cyclic nucleotide-binding domain-containing protein
  • FAP107/MC11
  • FAP129
  • FAP141
  • FAP21
  • FAP90
  • FAP95/MC6
  • FAP96B
  • FAP96C/MC15
  • Flagellar associated protein
  • Flagellar protofilament ribbon protein, putative
  • KIAA1430 homologue
  • MC3
  • MC4
  • MC5
  • MC7
  • MC8
  • MOP23A
  • MOP23B
  • MOP23C
  • Meiosis-specific nuclear structural protein 1
  • PACRGA
  • PACRGB
  • PBP36
  • PON3
  • PON4
  • Peptidyl-prolyl cis-trans isomerase
  • Rib72 protein-like protein
  • STOP axonemal protein
  • Starmaker
  • TbMIP23
  • TbRib26b
  • Tubulin alpha chain
  • Tubulin beta chain
KeywordsMOTOR PROTEIN / flagella / microtubule
Function / homology
Function and homology information


intraciliary transport particle / microtubule anchoring / cilium-dependent cell motility / regulation of cilium beat frequency involved in ciliary motility / axonemal microtubule / negative regulation of microtubule depolymerization / nucleoside-diphosphate kinase / ciliary plasm / nuclear lumen / UTP biosynthetic process ...intraciliary transport particle / microtubule anchoring / cilium-dependent cell motility / regulation of cilium beat frequency involved in ciliary motility / axonemal microtubule / negative regulation of microtubule depolymerization / nucleoside-diphosphate kinase / ciliary plasm / nuclear lumen / UTP biosynthetic process / CTP biosynthetic process / motile cilium / nucleoside diphosphate kinase activity / GTP biosynthetic process / positive regulation of cell motility / post-transcriptional regulation of gene expression / cyclosporin A binding / cortical cytoskeleton / phosphate ion binding / mitotic cytokinesis / axoneme / cilium assembly / alpha-tubulin binding / cytoplasmic microtubule / Hsp70 protein binding / mitotic spindle organization / meiotic cell cycle / RNA polymerase II CTD heptapeptide repeat P3 isomerase activity / RNA polymerase II CTD heptapeptide repeat P6 isomerase activity / peptidylprolyl isomerase / Hsp90 protein binding / structural constituent of cytoskeleton / microtubule cytoskeleton organization / mitotic spindle / protein folding / mitotic cell cycle / microtubule binding / microtubule / cytoskeleton / hydrolase activity / calmodulin binding / ciliary basal body / cilium / ribosome / GTPase activity / calcium ion binding / GTP binding / mitochondrion / nucleoplasm / ATP binding / metal ion binding / nucleus / cytoplasm
Similarity search - Function
Cilia- and flagella-associated protein 97 / Uncharacterized 22kDa protein in aldolase locus / Tubby, N-terminal / Hemingway/CFA97 / Hemingway/CFA97 / CCDC81, HU domain 1 / Protein of unknown function DUF4586 / CCDC81, HU domain 2 / CCDC81 eukaryotic HU domain 1 / Cilia-and flagella-associated protein 96 ...Cilia- and flagella-associated protein 97 / Uncharacterized 22kDa protein in aldolase locus / Tubby, N-terminal / Hemingway/CFA97 / Hemingway/CFA97 / CCDC81, HU domain 1 / Protein of unknown function DUF4586 / CCDC81, HU domain 2 / CCDC81 eukaryotic HU domain 1 / Cilia-and flagella-associated protein 96 / CCDC81 eukaryotic HU domain 2 / : / Cilia- and flagella-associated protein 161-like domain / : / Meiosis-specific nuclear structural protein 1 / Cilia- and flagella-associated protein 45 / NDPK7, second NDPk domain / Cilia- and flagella- associated protein 210 / CFAP53/TCHP / Trichohyalin-plectin-homology domain / Trichohyalin-plectin-homology domain / RIB43A / RIB43A / DM10 domain / EF-hand domain-containing protein EFHC1/EFHC2/EFHB / DM10 domain / DM10 domain profile. / Domains in hypothetical proteins in Drosophila, C. elegans and mammals. Occurs singly in some nucleoside diphosphate kinases. / Enkurin domain / : / Calmodulin-binding / Enkurin domain profile. / : / CFA20 domain / Cilia- and flagella-associated protein 20/CFAP20DC / CFA20 domain / Parkin co-regulated protein / Parkin co-regulated protein / Nucleoside diphosphate kinase-like domain / Nucleoside diphosphate kinase / NDK / Nucleoside diphosphate kinase-like domain superfamily / Quinoprotein alcohol dehydrogenase-like superfamily / Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain profile. / Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain / Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD / Cyclophilin-like domain superfamily / cAMP/cGMP binding motif profile. / Cyclic nucleotide-binding domain / Tubulin-beta mRNA autoregulation signal. / Alpha tubulin / Beta tubulin, autoregulation binding site / Beta tubulin / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain / Tubulin, conserved site / Tubulin subunits alpha, beta, and gamma signature. / Tubulin/FtsZ family, C-terminal domain / Tubulin/FtsZ-like, C-terminal domain / Tubulin/FtsZ, C-terminal / Tubulin/FtsZ, 2-layer sandwich domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ, GTPase domain / Tubulin/FtsZ, GTPase domain superfamily / EF-hand domain pair / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / Armadillo-type fold / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / WD domain, G-beta repeat / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / Peptidyl-prolyl cis-trans isomerase / Calpain-like cysteine peptidase, putative / Trichohyalin-plectin-homology domain-containing protein / CCDC81 HU domain-containing protein / Uncharacterized protein / Uncharacterized protein / EF-hand domain-containing protein / Uncharacterized protein ...GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / Peptidyl-prolyl cis-trans isomerase / Calpain-like cysteine peptidase, putative / Trichohyalin-plectin-homology domain-containing protein / CCDC81 HU domain-containing protein / Uncharacterized protein / Uncharacterized protein / EF-hand domain-containing protein / Uncharacterized protein / T. brucei spp.-specific protein / Cilia- and flagella-associated protein 52 / Uncharacterized protein / Flagellar associated protein / Uncharacterized protein / Enkurin domain-containing protein / Trichohyalin-plectin-homology domain-containing protein / Uncharacterized protein / DM10 domain-containing protein / Cyclic nucleotide-binding domain-containing protein / EF-hand domain-containing protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Rib72 protein-like protein / Uncharacterized protein / EF-hand domain-containing protein / KIAA1430 homologue / Uncharacterized protein / CFA20 domain-containing protein / Nucleoside diphosphate kinase, putative / Uncharacterized protein / T. brucei spp.-specific protein / EF-hand domain-containing protein / Tubulin alpha chain / Tubulin beta chain / Enkurin domain-containing protein / Uncharacterized protein / Flagellar protofilament ribbon protein, putative / Cilia- and flagella-associated protein 45 / Uncharacterized protein / Cilia- and flagella-associated protein 53 / EF-hand domain-containing protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / STOP axonemal protein / Uncharacterized protein / Starmaker / Uncharacterized protein / EF-hand domain-containing family member C2 / Uncharacterized protein / EF-hand domain-containing protein / Nucleoside diphosphate kinase, putative / Uncharacterized protein / Uncharacterized protein / Enkurin domain-containing protein / Enkurin domain-containing protein / Calcium-binding protein, putative / Uncharacterized protein / Meiosis-specific nuclear structural protein 1
Similarity search - Component
Biological speciesTrypanosoma brucei brucei TREU927 (eukaryote)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.8 Å
AuthorsXia, X. / Shimogawa, M.M. / Wang, H. / Liu, S. / Wijono, A. / Langousis, G. / Kassem, A.M. / Wohlschlegel, J.A. / Hill, K. / Zhou, Z.H.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01GM071940 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01AI052348 United States
CitationJournal: Science / Year: 2025
Title: Trypanosome doublet microtubule structures reveal flagellum assembly and motility mechanisms.
Authors: Xian Xia / Michelle M Shimogawa / Hui Wang / Samuel Liu / Angeline Wijono / Gerasimos Langousis / Ahmad M Kassem / James A Wohlschlegel / Kent L Hill / Z Hong Zhou /
Abstract: The flagellum of drives the parasite's characteristic screw-like motion and is essential for its replication, transmission, and pathogenesis. However, the molecular details of this process remain ...The flagellum of drives the parasite's characteristic screw-like motion and is essential for its replication, transmission, and pathogenesis. However, the molecular details of this process remain unclear. Here, we present high-resolution (up to 2.8 angstrom) cryo-electron microscopy structures of flagellar doublet microtubules (DMTs). Integrated modeling identified 154 different axonemal proteins inside and outside the DMT and, together with genetic and proteomic interrogation, revealed conserved and trypanosome-specific foundations of flagellum assembly and motility. We captured axonemal dynein motors in their pre-power stroke state. Comparing atomic models between pre- and post-power strokes defined how dynein structural changes drive sliding of adjacent DMTs during flagellar beating. This study illuminates structural dynamics underlying flagellar motility and identifies pathogen-specific proteins to consider for therapeutic interventions targeting neglected diseases.
History
DepositionOct 22, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 12, 2025Provider: repository / Type: Initial release
Revision 1.1Mar 26, 2025Group: Data collection / Database references / Category: citation / citation_author / em_admin
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name / _em_admin.last_update

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
0A: EF-hand domain-containing family member C2
0B: EF-hand domain-containing family member C2
0C: EF-hand domain-containing family member C2
0D: EF-hand domain-containing family member C2
0E: EF-hand domain-containing family member C2
0F: Rib72 protein-like protein
0G: CMF34/CARP4
0H: Flagellar protofilament ribbon protein, putative
0I: Flagellar protofilament ribbon protein, putative
0J: Flagellar protofilament ribbon protein, putative
0K: Flagellar protofilament ribbon protein, putative
0M: Cilia- and flagella-associated protein 53
0N: Cilia- and flagella-associated protein 53
0O: Meiosis-specific nuclear structural protein 1
0P: Meiosis-specific nuclear structural protein 1
0Q: Nucleoside diphosphate kinase, putative
0R: Nucleoside diphosphate kinase, putative
0S: EF-hand domain-containing protein
0T: EF-hand domain-containing protein
0U: Cyclic nucleotide-binding domain-containing protein
0V: TbMIP23
0W: FAP141
0X: EF-hand domain-containing protein
0Y: Calpain-like cysteine peptidase, putative
0Z: EF-hand domain-containing protein
1A: Calcium-binding protein, putative
1B: EF-hand domain-containing protein
1C: Peptidyl-prolyl cis-trans isomerase
1D: EF-hand domain-containing protein
1E: FAP107/MC11
1F: T. brucei spp.-specific protein
1G: FAP95/MC6
1H: FAP129
1I: T. brucei spp.-specific protein
1J: T. brucei spp.-specific protein
1K: FAP21
1L: FAP21
1M: Flagellar associated protein
1N: Flagellar associated protein
1O: TbRib26b
1P: TbRib26b
1Q: PACRGA
1R: PACRGA
1S: PACRGA
1T: PACRGB
1U: PACRGB
1V: Cilia- and flagella-associated protein 20
1W: Cilia- and flagella-associated protein 20
1X: Cilia- and flagella-associated protein 20
1Y: Cilia- and flagella-associated protein 20
1Z: Cilia- and flagella-associated protein 20
2A: Cilia- and flagella-associated protein 20
2B: Cilia- and flagella-associated protein 52
2C: Cilia- and flagella-associated protein 52
2D: Cilia- and flagella-associated protein 52
2E: Enkurin domain-containing protein
2F: Enkurin domain-containing protein
2G: Enkurin domain-containing protein
2H: Enkurin domain-containing protein
2I: MC4
2J: MC4
2K: MC4
2L: MC5
2M: MC5
2N: CCDC81 HU domain-containing protein
2O: Cilia- and flagella-associated protein 45
2P: Cilia- and flagella-associated protein 45
2Q: Cilia- and flagella-associated protein 45
2R: Cilia- and flagella-associated protein 45
2S: Trichohyalin-plectin-homology domain-containing protein
2T: Trichohyalin-plectin-homology domain-containing protein
2U: Trichohyalin-plectin-homology domain-containing protein
2V: Trichohyalin-plectin-homology domain-containing protein
2W: Trichohyalin-plectin-homology domain-containing protein
2X: Trichohyalin-plectin-homology domain-containing protein
2Y: Trichohyalin-plectin-homology domain-containing protein
2Z: Trichohyalin-plectin-homology domain-containing protein
3A: Trichohyalin-plectin-homology domain-containing protein
3B: Trichohyalin-plectin-homology domain-containing protein
3C: Trichohyalin-plectin-homology domain-containing protein
3D: Trichohyalin-plectin-homology domain-containing protein
3E: STOP axonemal protein
3F: STOP axonemal protein
3G: STOP axonemal protein
3H: STOP axonemal protein
3I: STOP axonemal protein
3J: STOP axonemal protein
3K: STOP axonemal protein
3L: STOP axonemal protein
3M: STOP axonemal protein
3N: STOP axonemal protein
3O: STOP axonemal protein
3P: STOP axonemal protein
3Q: MC8
3R: MC3
3S: FAP90
3T: PBP36
3U: PBP36
3V: Enkurin domain-containing protein
3W: Enkurin domain-containing protein
3X: Enkurin domain-containing protein
3Y: Enkurin domain-containing protein
3Z: Enkurin domain-containing protein
4A: Enkurin domain-containing protein
4B: PON3
4C: PON3
4D: PON3
4E: PON4
4F: PON4
4G: PON4
4H: MC7
4I: FAP96C/MC15
4J: FAP96C/MC15
4K: FAP96B
4L: FAP96B
4M: MOP23A
4N: MOP23A
4O: MOP23A
4P: MOP23B
4Q: MOP23C
4R: KIAA1430 homologue
4S: KIAA1430 homologue
4T: Starmaker
4U: Starmaker
4V: Starmaker
4W: Starmaker
4X: TbRib26b
4Y: KIAA1430 homologue
AA: Tubulin alpha chain
AB: Tubulin beta chain
AC: Tubulin alpha chain
AD: Tubulin beta chain
AE: Tubulin alpha chain
AF: Tubulin beta chain
AG: Tubulin alpha chain
AH: Tubulin beta chain
AI: Tubulin alpha chain
AJ: Tubulin beta chain
AK: Tubulin alpha chain
AL: Tubulin beta chain
AM: Tubulin alpha chain
AN: Tubulin beta chain
AO: Tubulin alpha chain
AP: Tubulin beta chain
AQ: Tubulin alpha chain
AR: Tubulin beta chain
AS: Tubulin alpha chain
AT: Tubulin beta chain
AU: Tubulin alpha chain
AV: Tubulin beta chain
AW: Tubulin alpha chain
AX: Tubulin beta chain
AY: Tubulin alpha chain
AZ: Tubulin beta chain
BA: Tubulin alpha chain
BB: Tubulin beta chain
BC: Tubulin alpha chain
BD: Tubulin beta chain
BE: Tubulin alpha chain
BF: Tubulin beta chain
BG: Tubulin alpha chain
BH: Tubulin beta chain
BI: Tubulin alpha chain
BJ: Tubulin beta chain
BK: Tubulin alpha chain
BL: Tubulin beta chain
BM: Tubulin alpha chain
BN: Tubulin beta chain
BO: Tubulin alpha chain
BP: Tubulin beta chain
BQ: Tubulin alpha chain
BR: Tubulin beta chain
BS: Tubulin alpha chain
BT: Tubulin beta chain
BU: Tubulin alpha chain
BV: Tubulin beta chain
BW: Tubulin alpha chain
BX: Tubulin alpha chain
BY: Tubulin beta chain
BZ: Tubulin alpha chain
CA: Tubulin beta chain
CB: Tubulin alpha chain
CC: Tubulin beta chain
CD: Tubulin alpha chain
CE: Tubulin beta chain
CF: Tubulin alpha chain
CG: Tubulin beta chain
CH: Tubulin alpha chain
CI: Tubulin beta chain
CJ: Tubulin alpha chain
CL: Tubulin beta chain
CM: Tubulin alpha chain
CN: Tubulin beta chain
CO: Tubulin alpha chain
CP: Tubulin beta chain
CQ: Tubulin alpha chain
CR: Tubulin beta chain
CS: Tubulin alpha chain
CT: Tubulin beta chain
CU: Tubulin alpha chain
CV: Tubulin beta chain
CW: Tubulin alpha chain
CX: Tubulin beta chain
CY: Tubulin alpha chain
CZ: Tubulin beta chain
DA: Tubulin alpha chain
DB: Tubulin beta chain
DC: Tubulin alpha chain
DD: Tubulin beta chain
DE: Tubulin alpha chain
DF: Tubulin beta chain
DG: Tubulin alpha chain
DH: Tubulin beta chain
DI: Tubulin alpha chain
DJ: Tubulin beta chain
DK: Tubulin alpha chain
DL: Tubulin beta chain
DM: Tubulin alpha chain
DN: Tubulin beta chain
DO: Tubulin alpha chain
DP: Tubulin beta chain
DQ: Tubulin alpha chain
DR: Tubulin beta chain
DS: Tubulin alpha chain
DT: Tubulin beta chain
DU: Tubulin alpha chain
DV: Tubulin beta chain
DW: Tubulin beta chain
DX: Tubulin alpha chain
DY: Tubulin beta chain
DZ: Tubulin alpha chain
EA: Tubulin beta chain
EB: Tubulin alpha chain
EC: Tubulin beta chain
ED: Tubulin alpha chain
EE: Tubulin beta chain
EF: Tubulin alpha chain
EG: Tubulin beta chain
EH: Tubulin alpha chain
EI: Tubulin beta chain
EJ: Tubulin alpha chain
EK: Tubulin beta chain
EL: Tubulin alpha chain
EM: Tubulin beta chain
EN: Tubulin alpha chain
EO: Tubulin beta chain
EP: Tubulin alpha chain
EQ: Tubulin beta chain
ER: Tubulin alpha chain
ES: Tubulin beta chain
ET: Tubulin alpha chain
EU: Tubulin beta chain
EV: Tubulin alpha chain
EW: Tubulin beta chain
EX: Tubulin alpha chain
EY: Tubulin beta chain
EZ: Tubulin alpha chain
FA: Tubulin beta chain
FB: Tubulin alpha chain
FC: Tubulin beta chain
FD: Tubulin alpha chain
FE: Tubulin beta chain
FF: Tubulin alpha chain
FG: Tubulin beta chain
FH: Tubulin alpha chain
FI: Tubulin beta chain
FJ: Tubulin alpha chain
FK: Tubulin beta chain
FL: Tubulin alpha chain
FM: Tubulin beta chain
FN: Tubulin alpha chain
FO: Tubulin beta chain
FP: Tubulin alpha chain
FQ: Tubulin beta chain
FR: Tubulin alpha chain
FS: Tubulin beta chain
FT: Tubulin alpha chain
FU: Tubulin alpha chain
FV: Tubulin beta chain
FW: Tubulin alpha chain
FX: Tubulin beta chain
FY: Tubulin alpha chain
FZ: Tubulin beta chain
GA: Tubulin alpha chain
GB: Tubulin beta chain
GC: Tubulin alpha chain
GD: Tubulin beta chain
GE: Tubulin alpha chain
GF: Tubulin beta chain
GG: Tubulin alpha chain
GH: Tubulin alpha chain
GI: Tubulin beta chain
GJ: Tubulin alpha chain
GK: Tubulin beta chain
GL: Tubulin alpha chain
GM: Tubulin beta chain
GN: Tubulin alpha chain
GO: Tubulin beta chain
GP: Tubulin alpha chain
GQ: Tubulin beta chain
GR: Tubulin alpha chain
GS: Tubulin beta chain
GT: Tubulin alpha chain
GU: Tubulin alpha chain
GV: Tubulin beta chain
GW: Tubulin alpha chain
GX: Tubulin beta chain
GY: Tubulin alpha chain
GZ: Tubulin beta chain
HA: Tubulin alpha chain
HB: Tubulin beta chain
HC: Tubulin alpha chain
HD: Tubulin beta chain
HE: Tubulin alpha chain
HF: Tubulin beta chain
HG: Tubulin alpha chain
HH: Tubulin beta chain
HI: Tubulin alpha chain
HJ: Tubulin beta chain
HK: Tubulin alpha chain
HL: Tubulin beta chain
HM: Tubulin alpha chain
HN: Tubulin beta chain
HO: Tubulin alpha chain
HP: Tubulin beta chain
HQ: Tubulin alpha chain
HR: Tubulin beta chain
HS: Tubulin beta chain
HT: Tubulin alpha chain
HU: Tubulin beta chain
HV: Tubulin alpha chain
HW: Tubulin beta chain
HX: Tubulin alpha chain
HY: Tubulin beta chain
HZ: Tubulin alpha chain
IA: Tubulin beta chain
IB: Tubulin alpha chain
IC: Tubulin beta chain
ID: Tubulin alpha chain
IE: Tubulin beta chain
IF: Tubulin beta chain
IG: Tubulin alpha chain
IH: Tubulin beta chain
II: Tubulin alpha chain
IJ: Tubulin beta chain
IK: Tubulin alpha chain
IL: Tubulin beta chain
IM: Tubulin alpha chain
IN: Tubulin beta chain
IO: Tubulin alpha chain
IP: Tubulin beta chain
IQ: Tubulin alpha chain
IR: Tubulin beta chain
IS: Tubulin beta chain
IT: Tubulin alpha chain
IU: Tubulin beta chain
IV: Tubulin alpha chain
IW: Tubulin beta chain
IX: Tubulin alpha chain
IY: Tubulin beta chain
IZ: Tubulin alpha chain
JA: Tubulin beta chain
JB: Tubulin alpha chain
JC: Tubulin beta chain
JD: Tubulin alpha chain
JE: Tubulin beta chain
JF: Tubulin alpha chain
JG: Tubulin beta chain
JH: Tubulin alpha chain
JI: Tubulin beta chain
JJ: Tubulin alpha chain
JK: Tubulin beta chain
JL: Tubulin alpha chain
JM: Tubulin beta chain
JN: Tubulin alpha chain
JO: Tubulin beta chain
JP: Tubulin alpha chain
JQ: Tubulin alpha chain
JR: Tubulin beta chain
JS: Tubulin alpha chain
JT: Tubulin beta chain
JU: Tubulin alpha chain
JV: Tubulin beta chain
JW: Tubulin alpha chain
JX: Tubulin beta chain
JY: Tubulin alpha chain
JZ: Tubulin beta chain
KA: Tubulin alpha chain
KB: Tubulin beta chain
KC: Tubulin alpha chain
KD: Tubulin alpha chain
KE: Tubulin beta chain
KF: Tubulin alpha chain
KG: Tubulin beta chain
KH: Tubulin alpha chain
KI: Tubulin beta chain
KJ: Tubulin alpha chain
KK: Tubulin beta chain
KL: Tubulin alpha chain
KM: Tubulin beta chain
KN: Tubulin alpha chain
KO: Tubulin beta chain
KP: Tubulin alpha chain
KQ: Tubulin alpha chain
KR: Tubulin beta chain
KS: Tubulin alpha chain
KT: Tubulin beta chain
KU: Tubulin alpha chain
KV: Tubulin beta chain
KW: Tubulin alpha chain
KX: Tubulin beta chain
KY: Tubulin alpha chain
KZ: Tubulin beta chain
LA: Tubulin alpha chain
LB: Tubulin beta chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)19,879,153871
Polymers19,735,263415
Non-polymers143,890456
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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EF-hand domain-containing ... , 8 types, 11 molecules 0A0B0C0D0E0S0T0X0Z1B1D

#1: Protein
EF-hand domain-containing family member C2


Mass: 86973.781 Da / Num. of mol.: 4 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q387A9
#2: Protein EF-hand domain-containing family member C2


Mass: 88366.906 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q57ZX1
#10: Protein EF-hand domain-containing protein


Mass: 47731.914 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q581Q7
#11: Protein EF-hand domain-containing protein


Mass: 48071.531 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q388A8
#15: Protein EF-hand domain-containing protein


Mass: 30499.936 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q57XA3
#17: Protein EF-hand domain-containing protein


Mass: 61839.383 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q383Y5
#19: Protein EF-hand domain-containing protein


Mass: 34213.496 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q38F14
#21: Protein EF-hand domain-containing protein


Mass: 36100.395 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q38AR7

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Protein , 38 types, 362 molecules 0F0G0H0I0J0K0O0P0U0V0W0Y1A1C1E1G1H1K1L1M1N1O1P4X1Q1R1S1T1U2I...

#3: Protein Rib72 protein-like protein


Mass: 82953.188 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q38AJ5
#4: Protein CMF34/CARP4


Mass: 90251.391 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
#5: Protein
Flagellar protofilament ribbon protein, putative


Mass: 46956.750 Da / Num. of mol.: 4 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q57UY7
#7: Protein Meiosis-specific nuclear structural protein 1


Mass: 52699.703 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q587B8
#12: Protein Cyclic nucleotide-binding domain-containing protein


Mass: 37578.066 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q387J0
#13: Protein TbMIP23


Mass: 23452.754 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q57XG0
#14: Protein FAP141


Mass: 14631.420 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q38BT0
#16: Protein Calpain-like cysteine peptidase, putative


Mass: 33172.227 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q381R3
#18: Protein Calcium-binding protein, putative


Mass: 41708.535 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q583R2
#20: Protein Peptidyl-prolyl cis-trans isomerase / PPIase


Mass: 30680.295 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: A0A1G4I9Z4, peptidylprolyl isomerase
#22: Protein FAP107/MC11


Mass: 28127.812 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q583W1
#24: Protein FAP95/MC6


Mass: 20151.945 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q389U0
#25: Protein FAP129


Mass: 42654.492 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q57Z34
#27: Protein FAP21


Mass: 46442.445 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q383S0
#28: Protein Flagellar associated protein


Mass: 45935.605 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q385B6
#29: Protein TbRib26b


Mass: 26226.729 Da / Num. of mol.: 3 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q384Q9
#30: Protein PACRGA


Mass: 33834.922 Da / Num. of mol.: 3 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q582U4
#31: Protein PACRGB


Mass: 35401.648 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q38E08
#36: Protein MC4


Mass: 40548.527 Da / Num. of mol.: 3 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q57XA7
#37: Protein MC5


Mass: 30760.701 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q385S6
#38: Protein CCDC81 HU domain-containing protein


Mass: 29888.291 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q383J9
#42: Protein
STOP axonemal protein


Mass: 30090.230 Da / Num. of mol.: 12 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q57YM5
#43: Protein MC8


Mass: 31647.955 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q386N3
#44: Protein MC3


Mass: 37327.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q38AQ1
#45: Protein FAP90


Mass: 21434.402 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q57ZR3
#46: Protein PBP36


Mass: 36147.027 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q57UM2
#49: Protein PON3


Mass: 46311.688 Da / Num. of mol.: 3 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q388F3
#50: Protein PON4


Mass: 37083.625 Da / Num. of mol.: 3 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q388F2
#51: Protein MC7


Mass: 37334.016 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q57YM4
#52: Protein FAP96C/MC15


Mass: 39428.738 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q57V66
#53: Protein FAP96B


Mass: 33435.266 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q384B8
#54: Protein MOP23A


Mass: 23471.566 Da / Num. of mol.: 3 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q582N6
#55: Protein MOP23B


Mass: 22494.564 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q383L7
#56: Protein MOP23C


Mass: 19407.205 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q580D2
#57: Protein KIAA1430 homologue


Mass: 19570.469 Da / Num. of mol.: 3 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q38AV7
#58: Protein
Starmaker


Mass: 95914.680 Da / Num. of mol.: 4 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q57ZC1
#59: Protein ...
Tubulin alpha chain


Mass: 49840.094 Da / Num. of mol.: 145 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q4GYY5
#60: Protein ...
Tubulin beta chain


Mass: 49747.926 Da / Num. of mol.: 142 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q4GYY6

-
Cilia- and flagella-associated protein ... , 4 types, 15 molecules 0M0N1V1W1X1Y1Z2A2B2C2D2O2P2Q2R

#6: Protein Cilia- and flagella-associated protein 53


Mass: 58689.828 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q57VE0
#32: Protein
Cilia- and flagella-associated protein 20


Mass: 34593.465 Da / Num. of mol.: 6 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q38C25
#33: Protein Cilia- and flagella-associated protein 52


Mass: 67770.891 Da / Num. of mol.: 3 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q384Q0
#39: Protein
Cilia- and flagella-associated protein 45


Mass: 58198.273 Da / Num. of mol.: 4 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q57UZ3

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Nucleoside diphosphate kinase, ... , 2 types, 2 molecules 0Q0R

#8: Protein Nucleoside diphosphate kinase, putative


Mass: 37147.473 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q38DQ0, nucleoside-diphosphate kinase
#9: Protein Nucleoside diphosphate kinase, putative


Mass: 38993.656 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q581Q9, nucleoside-diphosphate kinase

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T. brucei spp.-specific ... , 2 types, 3 molecules 1F1I1J

#23: Protein T. brucei spp.-specific protein


Mass: 28844.326 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q38EE4
#26: Protein T. brucei spp.-specific protein


Mass: 46540.539 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q384L6

-
Enkurin domain-containing ... , 4 types, 10 molecules 2E2F2G2H3V3W3X3Y3Z4A

#34: Protein Enkurin domain-containing protein


Mass: 30264.260 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q385T0
#35: Protein Enkurin domain-containing protein


Mass: 42281.645 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q4GZB9
#47: Protein Enkurin domain-containing protein


Mass: 31393.762 Da / Num. of mol.: 3 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q583F4
#48: Protein Enkurin domain-containing protein


Mass: 30823.730 Da / Num. of mol.: 3 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q583F5

-
Trichohyalin-plectin-homology domain-containing ... , 2 types, 12 molecules 2S2T2U2V2W2X2Y2Z3A3B3C3D

#40: Protein Trichohyalin-plectin-homology domain-containing protein


Mass: 61310.469 Da / Num. of mol.: 3 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q386E1
#41: Protein
Trichohyalin-plectin-homology domain-containing protein


Mass: 41736.418 Da / Num. of mol.: 9 / Source method: isolated from a natural source
Source: (natural) Trypanosoma brucei brucei TREU927 (eukaryote)
References: UniProt: Q383H7

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Non-polymers , 4 types, 456 molecules

#61: Chemical...
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 24 / Source method: obtained synthetically / Formula: Zn / Feature type: SUBJECT OF INVESTIGATION
#62: Chemical...
ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE


Mass: 523.180 Da / Num. of mol.: 145 / Source method: obtained synthetically / Formula: C10H16N5O14P3 / Feature type: SUBJECT OF INVESTIGATION / Comment: GTP, energy-carrying molecule*YM
#63: Chemical...
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 145 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#64: Chemical...
ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 142 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Feature type: SUBJECT OF INVESTIGATION / Comment: GDP, energy-carrying molecule*YM

-
Details

Has ligand of interestY
Has protein modificationN

-
Experimental details

-
Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: FILAMENT / 3D reconstruction method: single particle reconstruction

-
Sample preparation

ComponentName: Trypanosoma brucei flagellum / Type: ORGANELLE OR CELLULAR COMPONENT
Details: Demembraned flagella were split by mild protease treatment
Entity ID: #60, #59, #51-#52, #56-#58, #50, #55, #49, #54, #47-#48, #53, #46, #36, #38, #34, #37, #35, #41, #43, #42, #40, #44, #39, #45, #28, #21-#22, #20, #25, #16, #27, #26, #23, #19, #29, #32, ...Entity ID: #60, #59, #51-#52, #56-#58, #50, #55, #49, #54, #47-#48, #53, #46, #36, #38, #34, #37, #35, #41, #43, #42, #40, #44, #39, #45, #28, #21-#22, #20, #25, #16, #27, #26, #23, #19, #29, #32, #31, #30, #33, #8, #13, #12, #11, #10, #14, #9, #24, #18, #15, #17, #5-#7, #1-#4
Source: NATURAL
Molecular weightExperimental value: NO
Source (natural)Organism: Trypanosoma brucei brucei TREU927 (eukaryote)
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R2/1
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K

-
Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 81000 X / Nominal defocus max: 2400 nm / Nominal defocus min: 1600 nm / Cs: 2.7 mm / C2 aperture diameter: 50 µm / Alignment procedure: COMA FREE
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingAverage exposure time: 2 sec. / Electron dose: 45 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Num. of grids imaged: 2 / Num. of real images: 106694
EM imaging opticsEnergyfilter name: GIF Quantum LS / Energyfilter slit width: 20 eV

-
Processing

EM softwareName: PHENIX / Version: 1.19.2_4158: / Category: model refinement
CTF correctionType: PHASE FLIPPING ONLY
Particle selectionNum. of particles selected: 7830948
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 455012 / Num. of class averages: 1 / Symmetry type: POINT
Atomic model buildingProtocol: AB INITIO MODEL / Space: REAL

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