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- PDB-7sqc: Ciliary C1 central pair apparatus isolated from Chlamydomonas rei... -

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Basic information

Entry
Database: PDB / ID: 7sqc
TitleCiliary C1 central pair apparatus isolated from Chlamydomonas reinhardtii
Components
  • (Unknown protein) x 4
  • CPC1
  • Calmodulin
  • FAP101
  • FAP105
  • FAP108
  • FAP114
  • FAP119
  • FAP15
  • FAP194
  • FAP216
  • FAP219
  • FAP221
  • FAP227
  • FAP246
  • FAP266
  • FAP275
  • FAP279
  • FAP297
  • FAP305
  • FAP42
  • FAP46
  • FAP47
  • FAP54
  • FAP69
  • FAP7
  • FAP74
  • FAP76
  • FAP81
  • FAP99
  • Flagellar associated protein
  • Heat shock protein 70A
  • Hydin
  • PF16
  • PF6
  • Phosphopyruvate hydratase
  • Tubulin alpha
  • Tubulin beta
KeywordsSTRUCTURAL PROTEIN / cilia / microtubule
Function / homology
Function and homology information


axonemal central pair projection / axonemal central apparatus / axonemal central apparatus assembly / organelle / establishment of meiotic spindle localization / cilium movement involved in cell motility / cilium movement / guanylate kinase activity / axoneme assembly / calcium-dependent cysteine-type endopeptidase activity ...axonemal central pair projection / axonemal central apparatus / axonemal central apparatus assembly / organelle / establishment of meiotic spindle localization / cilium movement involved in cell motility / cilium movement / guanylate kinase activity / axoneme assembly / calcium-dependent cysteine-type endopeptidase activity / phosphopyruvate hydratase / phosphopyruvate hydratase complex / phosphopyruvate hydratase activity / adenylate kinase / adenylate kinase activity / motile cilium / spindle organization / myosin phosphatase activity / protein serine/threonine phosphatase activity / protein-serine/threonine phosphatase / axoneme / chaperone cofactor-dependent protein refolding / cilium assembly / enzyme regulator activity / protein folding chaperone / heat shock protein binding / tubulin binding / glycolytic process / electron transport chain / ATP-dependent protein folding chaperone / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / structural constituent of cytoskeleton / cilium / spindle pole / microtubule cytoskeleton organization / microtubule cytoskeleton / mitotic cell cycle / protein refolding / microtubule binding / microtubule / transcription coactivator activity / calmodulin binding / hydrolase activity / negative regulation of cell population proliferation / nucleotide binding / GTPase activity / calcium ion binding / regulation of DNA-templated transcription / GTP binding / magnesium ion binding / ATP hydrolysis activity / proteolysis / ATP binding / membrane / nucleus / metal ion binding / cytoplasm / cytosol
Similarity search - Function
Sperm-associated antigen 17 / Cilia- and flagella-associated protein 54 / Domain of unknown function DUF4456 / Domain of unknown function DUF4455 / Primary ciliary dyskinesia protein 1 / Flagellar C1a complex subunit C1a-32 / Deleted in lung and esophageal cancer protein 1 / Cilia- and flagella-associated protein 99 / Cilia- and flagella-associated protein 46 / Leucine-rich repeat-containing protein 72 ...Sperm-associated antigen 17 / Cilia- and flagella-associated protein 54 / Domain of unknown function DUF4456 / Domain of unknown function DUF4455 / Primary ciliary dyskinesia protein 1 / Flagellar C1a complex subunit C1a-32 / Deleted in lung and esophageal cancer protein 1 / Cilia- and flagella-associated protein 99 / Cilia- and flagella-associated protein 46 / Leucine-rich repeat-containing protein 72 / : / : / : / : / Domain of unknown function (DUF4455) / Domain of unknown function (DUF4456) / Flagellar C1a complex subunit C1a-32 / Cilia- and flagella-associated protein 54 / Cilia- and flagella-associated protein 69, ARM repeat / Associate of Myc 1 / Hydrocephalus-inducing-like / Flagellar-associated PapD-like / CH-like domain in sperm protein / CH-like domain in sperm protein / : / Adenylate kinase, active site lid domain superfamily / : / Peptidase C2, calpain, catalytic domain / Calpain family cysteine protease / Cysteine proteinase, calpain-type, catalytic domain profile. / Calpain-like thiol protease family. / Possible plasma membrane-binding motif in junctophilins, PIP-5-kinases and protein kinases. / MORN motif / MORN repeat / Serine-threonine protein phosphatase, N-terminal / Serine-threonine protein phosphatase N-terminal domain / Transglutaminase/protease-like homologues / Transglutaminase-like / Enolase / Enolase, conserved site / Enolase, C-terminal TIM barrel domain / Enolase, N-terminal / Enolase, C-terminal TIM barrel domain / Enolase, N-terminal domain / Enolase signature. / Enolase, C-terminal TIM barrel domain / Enolase, N-terminal domain / Adenylate kinase / Adenylate kinase, conserved site / Adenylate kinase signature. / Adenylate kinase/UMP-CMP kinase / Leucine rich repeat, ribonuclease inhibitor type / Leucine-rich repeat / Serine/threonine specific protein phosphatases signature. / Protein phosphatase 2A homologues, catalytic domain. / Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase / IQ calmodulin-binding motif / Guanylate kinase-like domain profile. / Guanylate kinase-like domain / Leucine-rich repeats, bacterial type / Heat shock hsp70 proteins family signature 2. / Heat shock hsp70 proteins family signature 1. / Heat shock hsp70 proteins family signature 3. / Heat shock protein 70, conserved site / Guanylate kinase/L-type calcium channel beta subunit / Guanylate kinase / Guanylate kinase homologues. / Heat shock protein 70kD, peptide-binding domain superfamily / Heat shock protein 70 family / Hsp70 protein / Calponin homology domain / Heat shock protein 70kD, C-terminal domain superfamily / Armadillo/beta-catenin-like repeat / Calponin homology (CH) domain / Leucine-rich repeat, SDS22-like subfamily / : / Short calmodulin-binding motif containing conserved Ile and Gln residues. / Enolase-like, N-terminal / Calponin homology domain / Enolase-like, C-terminal domain superfamily / CH domain superfamily / Calponin homology (CH) domain profile. / NADH dehydrogenase ubiquinone Fe-S protein 4, mitochondrial / Calcineurin-like phosphoesterase domain, ApaH type / Calcineurin-like phosphoesterase / IQ motif profile. / Armadillo/beta-catenin-like repeats / Armadillo / IQ motif, EF-hand binding site / Metallo-dependent phosphatase-like / Leucine rich repeat / Leucine-rich repeat, typical subtype / Leucine-rich repeats, typical (most populated) subfamily / Alpha tubulin / Tubulin-beta mRNA autoregulation signal. / Beta tubulin, autoregulation binding site / Beta tubulin / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / Calponin-homology (CH) domain-containing protein / Uncharacterized protein / EF-hand domain-containing protein / adenylate kinase / Flagellar associated protein / Spermatogenesis-associated protein 17 ...ADENOSINE-5'-DIPHOSPHATE / PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / Calponin-homology (CH) domain-containing protein / Uncharacterized protein / EF-hand domain-containing protein / adenylate kinase / Flagellar associated protein / Spermatogenesis-associated protein 17 / Flagellar associated protein / Sperm-associated antigen 6 / Flagellar associated protein / Flagellar associated protein / Flagellar associated protein / Cilia- and flagella-associated protein 69 ARM repeats domain-containing protein / Uncharacterized protein / Minichromosome loss protein Mcl1 middle region domain-containing protein / Flagellar associated protein 174 / Cilia- and flagella-associated protein 46 / Calmodulin / Predicted protein / Cilia- and flagella-associated protein 99 / Uncharacterized protein / Cilia- and flagella-associated protein 54 / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / phosphopyruvate hydratase / FAP221 / Cilia- and flagella-associated protein 74 / Tubulin beta-1/beta-2 chain / Tubulin alpha-1 chain / Central apparatus associated protein C1a-86 / Central apparatus associated protein C1a-34 / Central apparatus associated protein C1a-32 / Central apparatus associated protein C1a-18 / Central pair complex 1 / PF6 protein / Serine/threonine-protein phosphatase
Similarity search - Component
Biological speciesChlamydomonas reinhardtii (plant)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.8 Å
AuthorsGui, M. / Wang, X. / Dutcher, S.K. / Brown, A. / Zhang, R.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) United States
CitationJournal: Nat Struct Mol Biol / Year: 2022
Title: Ciliary central apparatus structure reveals mechanisms of microtubule patterning.
Authors: Miao Gui / Xiangli Wang / Susan K Dutcher / Alan Brown / Rui Zhang /
Abstract: A pair of extensively modified microtubules form the central apparatus (CA) of the axoneme of most motile cilia, where they regulate ciliary motility. The external surfaces of both CA microtubules ...A pair of extensively modified microtubules form the central apparatus (CA) of the axoneme of most motile cilia, where they regulate ciliary motility. The external surfaces of both CA microtubules are patterned asymmetrically with large protein complexes that repeat every 16 or 32 nm. The composition of these projections and the mechanisms that establish asymmetry and longitudinal periodicity are unknown. Here, by determining cryo-EM structures of the CA microtubules, we identify 48 different CA-associated proteins, which in turn reveal mechanisms for asymmetric and periodic protein binding to microtubules. We identify arc-MIPs, a novel class of microtubule inner protein, that bind laterally across protofilaments and remodel tubulin structure and lattice contacts. The binding mechanisms utilized by CA proteins may be generalizable to other microtubule-associated proteins. These structures establish a foundation to elucidate the contributions of individual CA proteins to ciliary motility and ciliopathies.
History
DepositionNov 5, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 13, 2022Provider: repository / Type: Initial release
Revision 1.1Jun 8, 2022Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID
Revision 1.2Jun 5, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
0A: Flagellar associated protein
0B: Flagellar associated protein
0C: Flagellar associated protein
0D: Flagellar associated protein
0E: Flagellar associated protein
0F: Flagellar associated protein
0G: Flagellar associated protein
0H: Flagellar associated protein
0I: Flagellar associated protein
0J: Flagellar associated protein
0K: Flagellar associated protein
0L: Flagellar associated protein
1A: FAP42
1B: FAP42
1C: FAP42
1D: FAP42
1F: FAP7
1G: FAP7
1H: FAP7
1I: FAP7
1J: FAP7
1K: FAP7
1L: FAP7
1M: FAP7
1N: FAP7
1O: FAP7
1P: FAP7
1Q: FAP7
1R: FAP7
1S: FAP7
1T: FAP7
1U: FAP7
1V: FAP7
1W: FAP7
1X: FAP7
1Y: FAP7
2A: FAP81
2B: FAP81
2E: FAP216
2F: FAP216
2H: FAP297
2I: FAP297
2K: FAP114
2L: FAP114
2M: FAP114
2N: FAP114
2O: FAP114
2P: FAP114
2Q: FAP114
3A: FAP305
3B: FAP305
3C: FAP305
3D: FAP305
3K: FAP119
3L: FAP119
3M: FAP119
3N: FAP119
3O: FAP119
3P: FAP119
4A: Calmodulin
4B: Calmodulin
4C: Calmodulin
4D: Calmodulin
4E: Calmodulin
4F: Calmodulin
4G: Calmodulin
4H: Calmodulin
4I: Calmodulin
4J: Calmodulin
4K: Calmodulin
4L: Calmodulin
5A: FAP101
5B: FAP101
5C: FAP101
5D: FAP101
6A: FAP15
6B: FAP15
6C: FAP15
6D: FAP15
7A: FAP227
7B: FAP227
7C: FAP227
7D: FAP227
7E: FAP227
7F: FAP227
7G: FAP227
7H: FAP227
7I: FAP227
7J: FAP227
7K: FAP227
7L: FAP227
8A: FAP105
8B: FAP105
8C: FAP105
8D: FAP105
9A: PF6
9B: PF6
9C: PF6
9D: PF6
9E: PF6
9F: PF6
A0: FAP219
A1: FAP219
A2: FAP219
A3: FAP219
A4: FAP219
B0: FAP99
B1: FAP99
B2: FAP99
C0: CPC1
C1: CPC1
C2: CPC1
C3: CPC1
C4: CPC1
D0: PF16
D1: PF16
D2: PF16
D3: PF16
D4: PF16
D5: PF16
D6: PF16
D7: PF16
E0: FAP108
E1: FAP108
E2: FAP108
E3: FAP108
F0: Hydin
F1: Hydin
F2: Hydin
F3: Hydin
G0: PF16
G1: PF16
G2: PF16
G3: PF16
G4: PF16
G5: PF16
H0: PF16
H1: PF16
H2: PF16
H3: PF16
H4: PF16
H5: PF16
H6: PF16
H7: PF16
I0: PF16
I1: PF16
J0: PF16
J1: PF16
J2: PF16
J3: PF16
K0: PF16
K1: PF16
K2: PF16
K3: PF16
L0: PF16
L1: PF16
L2: PF16
L3: PF16
M0: FAP221
M1: FAP221
N0: FAP194
N1: FAP194
N2: FAP194
N3: FAP194
NB: Tubulin alpha
NC: Tubulin beta
ND: Tubulin alpha
NE: Tubulin beta
NF: Tubulin alpha
NG: Tubulin beta
NH: Tubulin alpha
NI: Tubulin beta
NJ: Tubulin alpha
NK: Tubulin beta
NL: Tubulin alpha
NM: Tubulin beta
NN: Tubulin alpha
NO: Tubulin beta
O0: FAP74
O1: FAP74
O2: FAP74
OC: Tubulin beta
OD: Tubulin alpha
OE: Tubulin beta
OF: Tubulin alpha
OG: Tubulin beta
OH: Tubulin alpha
OI: Tubulin beta
OJ: Tubulin alpha
OK: Tubulin beta
OL: Tubulin alpha
OM: Tubulin beta
ON: Tubulin alpha
OO: Tubulin beta
OP: Tubulin alpha
OQ: Tubulin beta
P0: FAP69
P1: FAP69
P2: FAP69
P3: FAP69
PC: Tubulin beta
PD: Tubulin alpha
PE: Tubulin beta
PF: Tubulin alpha
PG: Tubulin beta
PH: Tubulin alpha
PI: Tubulin beta
PJ: Tubulin alpha
PK: Tubulin beta
PL: Tubulin alpha
PM: Tubulin beta
PN: Tubulin alpha
PO: Tubulin beta
PP: Tubulin alpha
PQ: Tubulin beta
Q0: FAP54
Q1: FAP54
QC: Tubulin beta
QD: Tubulin alpha
QE: Tubulin beta
QF: Tubulin alpha
QG: Tubulin beta
QH: Tubulin alpha
QI: Tubulin beta
QJ: Tubulin alpha
QK: Tubulin beta
QL: Tubulin alpha
QM: Tubulin beta
QN: Tubulin alpha
QO: Tubulin beta
QP: Tubulin alpha
QQ: Tubulin beta
R0: FAP46
R1: FAP46
RC: Tubulin beta
RD: Tubulin alpha
RE: Tubulin beta
RF: Tubulin alpha
RG: Tubulin beta
RH: Tubulin alpha
RI: Tubulin beta
RJ: Tubulin alpha
RK: Tubulin beta
RL: Tubulin alpha
RM: Tubulin beta
RN: Tubulin alpha
RO: Tubulin beta
RP: Tubulin alpha
S0: FAP275
S1: FAP275
S2: FAP275
S3: FAP275
S5: Unknown protein
SB: Tubulin alpha
SC: Tubulin beta
SD: Tubulin alpha
SE: Tubulin beta
SF: Tubulin alpha
SG: Tubulin beta
SH: Tubulin alpha
SI: Tubulin beta
SJ: Tubulin alpha
SK: Tubulin beta
SL: Tubulin alpha
SM: Tubulin beta
SN: Tubulin alpha
SO: Tubulin beta
SP: Tubulin alpha
T0: FAP47
T1: FAP47
T2: FAP47
T3: FAP47
TB: Tubulin alpha
TC: Tubulin beta
TD: Tubulin alpha
TE: Tubulin beta
TF: Tubulin alpha
TG: Tubulin beta
TH: Tubulin alpha
TI: Tubulin beta
TJ: Tubulin alpha
TK: Tubulin beta
TL: Tubulin alpha
TM: Tubulin beta
TN: Tubulin alpha
TO: Tubulin beta
TP: Tubulin alpha
U0: FAP279
U1: FAP279
UB: Tubulin alpha
UC: Tubulin beta
UD: Tubulin alpha
UE: Tubulin beta
UF: Tubulin alpha
UG: Tubulin beta
UH: Tubulin alpha
UI: Tubulin beta
UJ: Tubulin alpha
UK: Tubulin beta
UL: Tubulin alpha
UM: Tubulin beta
UN: Tubulin alpha
UO: Tubulin beta
UP: Tubulin alpha
V0: FAP266
V1: FAP266
VB: Tubulin alpha
VC: Tubulin beta
VD: Tubulin alpha
VE: Tubulin beta
VF: Tubulin alpha
VG: Tubulin beta
VH: Tubulin alpha
VI: Tubulin beta
VJ: Tubulin alpha
VK: Tubulin beta
VL: Tubulin alpha
VM: Tubulin beta
VN: Tubulin alpha
VO: Tubulin beta
VP: Tubulin alpha
W0: FAP76
W1: FAP76
W3: Unknown protein
W4: Unknown protein
W5: Unknown protein
W6: Unknown protein
W7: Unknown protein
W8: Unknown protein
W9: Unknown protein
WA: Tubulin beta
WB: Tubulin alpha
WC: Tubulin beta
WD: Tubulin alpha
WE: Tubulin beta
WF: Tubulin alpha
WG: Tubulin beta
WH: Tubulin alpha
WI: Tubulin beta
WJ: Tubulin alpha
WK: Tubulin beta
WL: Tubulin alpha
WM: Tubulin beta
WN: Tubulin alpha
WO: Tubulin beta
X0: FAP246
X1: FAP246
X2: FAP246
X3: FAP246
XA: Tubulin beta
XB: Tubulin alpha
XC: Tubulin beta
XD: Tubulin alpha
XE: Tubulin beta
XF: Tubulin alpha
XG: Tubulin beta
XH: Tubulin alpha
XI: Tubulin beta
XJ: Tubulin alpha
XK: Tubulin beta
XL: Tubulin alpha
XM: Tubulin beta
XN: Tubulin alpha
XO: Tubulin beta
Y0: Phosphopyruvate hydratase
Y1: Phosphopyruvate hydratase
Y2: Phosphopyruvate hydratase
Y3: Phosphopyruvate hydratase
Y4: Phosphopyruvate hydratase
Y5: Phosphopyruvate hydratase
Y6: Phosphopyruvate hydratase
Y7: Phosphopyruvate hydratase
YB: Tubulin alpha
YC: Tubulin beta
YD: Tubulin alpha
YE: Tubulin beta
YF: Tubulin alpha
YG: Tubulin beta
YH: Tubulin alpha
YI: Tubulin beta
YJ: Tubulin alpha
YK: Tubulin beta
YL: Tubulin alpha
YM: Tubulin beta
YN: Tubulin alpha
YO: Tubulin beta
YP: Tubulin alpha
Z0: Heat shock protein 70A
Z1: Heat shock protein 70A
Z2: Heat shock protein 70A
Z3: Heat shock protein 70A
ZB: Tubulin alpha
ZC: Tubulin beta
ZD: Tubulin alpha
ZE: Tubulin beta
ZF: Tubulin alpha
ZG: Tubulin beta
ZH: Tubulin alpha
ZI: Tubulin beta
ZJ: Tubulin alpha
ZK: Tubulin beta
ZL: Tubulin alpha
ZM: Tubulin beta
ZN: Tubulin alpha
ZO: Tubulin beta
ZP: Tubulin alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,563,822708
Polymers27,462,411406
Non-polymers101,412302
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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Protein , 40 types, 405 molecules 0A0B0C0D0E0F0G0H0I0J0K0L1A1B1C1D1F1G1H1I1J1K1L1M1N1O1P1Q1R1S...

#1: Protein
Flagellar associated protein / Flagellar associated protein 174


Mass: 10336.616 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8I439
#2: Protein
FAP42 / Adenylate kinase


Mass: 269172.500 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A0A2K3D425, adenylate kinase
#3: Protein
FAP7 / Flagella associated protein


Mass: 54721.914 Da / Num. of mol.: 20 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8IVW2
#4: Protein FAP81


Mass: 234483.781 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A0A2K3DQM4
#5: Protein FAP216 / Flagellar associated protein


Mass: 79183.719 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8JGM3
#6: Protein FAP297


Mass: 99187.336 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A0A2K3E6N2
#7: Protein
FAP114 / Flagellar associated protein C1a-32 / Central apparatus associated protein C1a-32


Mass: 31575.461 Da / Num. of mol.: 7 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q45QX5
#8: Protein
FAP305


Mass: 47031.668 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A0A2K3D8V0
#9: Protein
FAP119 / Flagellar associated protein / Central apparatus associated protein C1a-34


Mass: 33850.367 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q45QX4
#10: Protein
Calmodulin


Mass: 18317.215 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8IDP6
#11: Protein
FAP101 / Central apparatus associated protein C1a-86


Mass: 85796.789 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q45QX3
#12: Protein
FAP15 / Serine/threonine-protein phosphatase


Mass: 34888.031 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
References: UniProt: Q9XGU3, protein-serine/threonine phosphatase
#13: Protein
FAP227 / Central apparatus associated protein C1a-18


Mass: 19550.742 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q45QX6
#14: Protein
FAP105


Mass: 31382.559 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8IKV8
#15: Protein
PF6 / PF6 protein / Flagellar central pair-associated protein


Mass: 237723.016 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q9ATK5
#16: Protein
FAP219


Mass: 29104.484 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
#17: Protein FAP99 / Cilia- and flagella-associated protein 99


Mass: 90340.258 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8IUG5
#18: Protein
CPC1 / Adenylate kinase


Mass: 205400.188 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: Q6J4H1, adenylate kinase
#19: Protein ...
PF16


Mass: 54710.590 Da / Num. of mol.: 36 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A0A2K3DEG1
#20: Protein
FAP108


Mass: 47789.062 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A0A2K3DQN7
#21: Protein
Hydin


Mass: 528934.062 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A0A2K3E6E5
#22: Protein FAP221


Mass: 103833.531 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: D4P3R6
#23: Protein
FAP194


Mass: 57764.508 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A0A2K3D452
#24: Protein ...
Tubulin alpha / Tubulin alpha-1 chain


Mass: 49638.008 Da / Num. of mol.: 97 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: P09204
#25: Protein ...
Tubulin beta / Tubulin beta-1/beta-2 chain / Beta-tubulin


Mass: 49665.809 Da / Num. of mol.: 96 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: P04690
#26: Protein FAP74 / Flagella-associated protein 74 / Cilia- and flagella-associated protein 74


Mass: 204036.094 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: D4P3R7
#27: Protein
FAP69


Mass: 114362.844 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A0A2K3DWV9
#28: Protein FAP54 / Flagella-associated protein 54


Mass: 332696.375 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8J666
#29: Protein FAP46 / Cilia- and flagella-associated protein 46


Mass: 289610.406 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8ICS9
#30: Protein
FAP275 / Flagellar associated protein


Mass: 18171.365 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8J870
#32: Protein
FAP47 / Calponin-homology (CH) domain-containing protein


Mass: 319999.812 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A0A2K3CP55
#33: Protein FAP279


Mass: 43267.051 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A0A2K3DN67
#34: Protein FAP266


Mass: 81663.047 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A0A2K3CU78
#35: Protein FAP76


Mass: 172707.297 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A0A2K3DDV4
#36: Protein
Unknown protein


Mass: 5805.147 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
#37: Protein Unknown protein


Mass: 12698.645 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
#38: Protein Unknown protein


Mass: 4358.364 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)
#39: Protein
FAP246


Mass: 120452.891 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A0A2K3CXT1
#40: Protein
Phosphopyruvate hydratase


Mass: 51664.762 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8JH98, phosphopyruvate hydratase
#41: Protein
Heat shock protein 70A


Mass: 71303.758 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant) / References: UniProt: A8JEU4, EC: 3.6.1.3

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Protein/peptide , 1 types, 1 molecules S5

#31: Protein/peptide Unknown protein


Mass: 3252.000 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Chlamydomonas reinhardtii (plant)

-
Non-polymers , 5 types, 302 molecules

#42: Chemical
ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#43: Chemical
ChemComp-ANP / PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER


Mass: 506.196 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C10H17N6O12P3 / Comment: AMP-PNP, energy-carrying molecule analogue*YM
#44: Chemical...
ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE


Mass: 523.180 Da / Num. of mol.: 97 / Source method: obtained synthetically / Formula: C10H16N5O14P3 / Comment: GTP, energy-carrying molecule*YM
#45: Chemical...
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 97 / Source method: obtained synthetically / Formula: Mg
#46: Chemical...
ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 96 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM

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Details

Has ligand of interestN

-
Experimental details

-
Experiment

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

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Sample preparation

ComponentName: C1 central pair apparatus complex / Type: COMPLEX / Entity ID: #1-#41 / Source: NATURAL
Molecular weightExperimental value: NO
Source (natural)Organism: Chlamydomonas reinhardtii (plant)
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

-
Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 3000 nm / Nominal defocus min: 500 nm / Alignment procedure: COMA FREE
Specimen holderCryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingElectron dose: 39.6 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

-
Processing

EM software
IDNameVersionCategory
7Coot0.9.5model fitting
9PHENIX1.19.2model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 80007 / Symmetry type: POINT

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