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- EMDB-55043: CM1-activated gTuRC in complex with nascent alpha-E254D mutant mi... -

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Basic information

Entry
Database: EMDB / ID: EMD-55043
TitleCM1-activated gTuRC in complex with nascent alpha-E254D mutant microtubules
Map dataConsensus map
Sample
  • Complex: gamma-tubulin ring complex
    • Protein or peptide: x 12 types
  • Ligand: x 1 types
KeywordsMicrotubule / cytoskeleton / g-tubulin ring complex / tubulin / STRUCTURAL PROTEIN / CDK5RAP2 / CM1 / nucleation
Function / homology
Function and homology information


basal body patch / protein localization to astral microtubule / protein localization to mitotic spindle / cortical microtubule cytoskeleton / tight junction assembly / mitotic spindle astral microtubule end / netrin receptor binding / microtubule nucleation by interphase microtubule organizing center / gamma-tubulin complex localization / microtubule nucleator activity ...basal body patch / protein localization to astral microtubule / protein localization to mitotic spindle / cortical microtubule cytoskeleton / tight junction assembly / mitotic spindle astral microtubule end / netrin receptor binding / microtubule nucleation by interphase microtubule organizing center / gamma-tubulin complex localization / microtubule nucleator activity / negative regulation of centriole replication / regulation of mitotic cell cycle spindle assembly checkpoint / protein localization to microtubule / dorsal root ganglion development / Post-chaperonin tubulin folding pathway / SUMO is conjugated to E1 (UBA2:SAE1) / SUMOylation of nuclear envelope proteins / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / Cilium Assembly / microtubule organizing center organization / cytoskeleton-dependent intracellular transport / SUMO is proteolytically processed / polar microtubule / Carboxyterminal post-translational modifications of tubulin / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / SUMOylation of transcription factors / interphase microtubule organizing center / gamma-tubulin complex / profilin binding / gamma-tubulin ring complex / Postmitotic nuclear pore complex (NPC) reformation / SUMOylation of transcription cofactors / septin ring / cell projection membrane / microtubule plus-end / SUMOylation of DNA damage response and repair proteins / mitotic spindle microtubule / protein localization to bicellular tight junction / meiotic spindle organization / Sealing of the nuclear envelope (NE) by ESCRT-III / Intraflagellar transport / Transcriptional and post-translational regulation of MITF-M expression and activity / SUMOylation of DNA replication proteins / regulation of transepithelial transport / attachment of mitotic spindle microtubules to kinetochore / morphogenesis of a polarized epithelium / microtubule nucleation / structural constituent of postsynaptic actin cytoskeleton / Formation of annular gap junctions / Formation of tubulin folding intermediates by CCT/TriC / Formation of the dystrophin-glycoprotein complex (DGC) / Gap junction degradation / Cell-extracellular matrix interactions / dense body / SUMOylation of SUMOylation proteins / microtubule plus-end binding / Gap junction assembly / microtubule bundle formation / regulation of stress fiber assembly / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / non-motile cilium assembly / gamma-tubulin binding / Regulation of CDH1 Function / Kinesins / non-motile cilium / protein localization to centrosome / Prefoldin mediated transfer of substrate to CCT/TriC / SUMOylation of RNA binding proteins / Adherens junctions interactions / Assembly and cell surface presentation of NMDA receptors / COPI-independent Golgi-to-ER retrograde traffic / Sensory processing of sound by outer hair cells of the cochlea / SUMOylation of chromatin organization proteins / regulation of neuron differentiation / centrosome cycle / regulation of focal adhesion assembly / Sensory processing of sound by inner hair cells of the cochlea / Interaction between L1 and Ankyrins / COPI-dependent Golgi-to-ER retrograde traffic / sarcomere organization / apical junction complex / negative regulation of neuron differentiation / positive regulation of wound healing / mitotic spindle pole / spindle midzone / negative regulation of microtubule polymerization / establishment of mitotic spindle orientation / maintenance of blood-brain barrier / filamentous actin / pericentriolar material / NuA4 histone acetyltransferase complex / centriole replication / ciliary transition zone / cell leading edge / Recycling pathway of L1 / myofibril / microtubule polymerization / microtubule organizing center / mitotic sister chromatid segregation / ubiquitin-like protein ligase binding
Similarity search - Function
CDK5 regulatory subunit-associated protein 2 / : / CDK5 regulatory subunit-associated protein 2-like, coiled coil / MOZART2 family / Mitotic-spindle organizing gamma-tubulin ring associated / Centrosomin, N-terminal motif 1 / Centrosomin N-terminal motif 1 / Mitotic-spindle organizing protein 1 / Mitotic-spindle organizing gamma-tubulin ring associated / EB1, C-terminal ...CDK5 regulatory subunit-associated protein 2 / : / CDK5 regulatory subunit-associated protein 2-like, coiled coil / MOZART2 family / Mitotic-spindle organizing gamma-tubulin ring associated / Centrosomin, N-terminal motif 1 / Centrosomin N-terminal motif 1 / Mitotic-spindle organizing protein 1 / Mitotic-spindle organizing gamma-tubulin ring associated / EB1, C-terminal / Microtubule-associated protein RP/EB / EB1, C-terminal domain superfamily / EB1-C terminal (EB1-C) domain profile. / : / EB1-like C-terminal motif / Gamma-tubulin complex component 6, N-terminal / Gamma-tubulin complex component 6 N-terminus / Gamma tubulin / Gamma tubulin complex component, C-terminal / Gamma-tubulin complex component, C-terminal domain superfamily / Gamma tubulin complex component C-terminal / Gamma-tubulin complex component protein / Gamma tubulin complex component protein, N-terminal / Gamma tubulin complex component N-terminal / Rad60/SUMO-like domain / Ubiquitin-2 like Rad60 SUMO-like / Calponin homology (CH) domain / Calponin homology domain / CH domain superfamily / Calponin homology (CH) domain profile. / Alpha tubulin / Tubulin-beta mRNA autoregulation signal. / Beta tubulin, autoregulation binding site / Actins signature 1. / Beta tubulin / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain / Tubulin, conserved site / Tubulin subunits alpha, beta, and gamma signature. / Actin / Actin family / Actin / 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 / ATPase, nucleotide binding domain / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily
Similarity search - Domain/homology
Tubulin gamma-1 chain / Actin, cytoplasmic 2 / Tubulin alpha-1B chain / Mitotic-spindle organizing protein 1 / Small ubiquitin-related modifier / Tubulin beta-3 chain / Microtubule-associated protein RP/EB family member 1 / Mitotic-spindle organizing protein 2A / Gamma-tubulin complex component 3 / Gamma-tubulin complex component 6 ...Tubulin gamma-1 chain / Actin, cytoplasmic 2 / Tubulin alpha-1B chain / Mitotic-spindle organizing protein 1 / Small ubiquitin-related modifier / Tubulin beta-3 chain / Microtubule-associated protein RP/EB family member 1 / Mitotic-spindle organizing protein 2A / Gamma-tubulin complex component 3 / Gamma-tubulin complex component 6 / Gamma-tubulin complex component 5 / CDK5 regulatory subunit-associated protein 2 / Gamma-tubulin complex component 2 / Gamma-tubulin complex component 4
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.67 Å
AuthorsLlorca O / Serna M / Lopez-Perrote A
Funding support Spain, European Union, 2 items
OrganizationGrant numberCountry
Agencia Estatal de Investigacion (AEI)MCIN/AEI/10.13039/501100011033 Spain
European Regional Development FundPID2023-146110NB-I00European Union
CitationJournal: Nat Commun / Year: 2026
Title: Structural basis of human γTuRC closure during CM1-activated microtubule nucleation.
Authors: Marina Serna / Cláudia Brito / Silvia Speroni / Fabian Zimmermann / Andrés Lopez-Perrote / Maria Gili / Cristina Lacasa / Jens Lüders / Thomas Surrey / Oscar Llorca /
Abstract: Microtubule nucleation by the γ-tubulin ring complex (γTuRC) is spatiotemporally regulated and in higher eukaryotes is thought to involve a transition from an inactive open to an active closed ...Microtubule nucleation by the γ-tubulin ring complex (γTuRC) is spatiotemporally regulated and in higher eukaryotes is thought to involve a transition from an inactive open to an active closed conformation that matches the microtubule geometry. However, γTuRC activators only promote a partially closed conformation, raising the question of whether complete closure is required for activation. Combining in vitro nucleation assays and cryo-EM, we find that centrosomin motif 1 (CM1), a conserved element of several γTuRC regulators, potently accelerates human γTuRC-mediated microtubule nucleation by facilitating complete closure of γTuRC as the nascent microtubule assembles. A 3.7 Å cryo-EM structure identifies the γTuRC latch and several interactions involved in conformational closure. Notably, the distinct subunits that keep γTuRC open and inactive in higher eukaryotes also participate in its closure and activation. This work provides additional insight into the logic of the human γTuRC architecture and its activation by CM1.
History
DepositionSep 9, 2025-
Header (metadata) releaseMay 13, 2026-
Map releaseMay 13, 2026-
UpdateJun 3, 2026-
Current statusJun 3, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_55043.png

Downloads & links

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Map

FileDownload / File: emd_55043.map.gz / Format: CCP4 / Size: 614.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationConsensus map
Projections & slices

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AxesZ (Sec.)Y (Row.)X (Col.)
1.06 Å/pix.
x 544 pix.
= 576.64 Å		1.06 Å/pix.
x 544 pix.
= 576.64 Å		1.06 Å/pix.
x 544 pix.
= 576.64 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.06 Å
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Contour LevelBy AUTHOR: 0.0035
Minimum - Maximum-0.0048037297 - 0.018327953
Average (Standard dev.)-0.00015725355 (±0.00083585107)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions544544544
Spacing544544544
CellA=B=C: 576.63995 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_55043_msk_1.map
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Additional map: Focused refined map for the modules in spokes 3, 5 and 7

Fileemd_55043_additional_1.map
AnnotationFocused refined map for the modules in spokes 3, 5 and 7
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Additional map: Consensus map sharpened using deepEMhancer

Fileemd_55043_additional_2.map
AnnotationConsensus map sharpened using deepEMhancer
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Additional map: Focused refined map for the module in spoke 13

Fileemd_55043_additional_3.map
AnnotationFocused refined map for the module in spoke 13
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Additional map: Sharpened focused refined map for the modules in...

Fileemd_55043_additional_4.map
AnnotationSharpened focused refined map for the modules in spokes 3, 5 and 7 using deepEMhancer
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Additional map: Sharpened focused refined map for the module in...

Fileemd_55043_additional_5.map
AnnotationSharpened focused refined map for the module in spoke 13 using deepEMhancer
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Additional map: Sharpened consensus map

Fileemd_55043_additional_6.map
AnnotationSharpened consensus map
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Additional map: Sharpened focused refined map for the gTuRC seam using deepEMhancer

Fileemd_55043_additional_7.map
AnnotationSharpened focused refined map for the gTuRC seam using deepEMhancer
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Additional map: Focused refined map for the gTuRC seam

Fileemd_55043_additional_8.map
AnnotationFocused refined map for the gTuRC seam
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Half map: Half 1 map of the consensus refinement

Fileemd_55043_half_map_1.map
AnnotationHalf 1 map of the consensus refinement
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Half map: Half 2 map of the consensus refinement

Fileemd_55043_half_map_2.map
AnnotationHalf 2 map of the consensus refinement
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Sample components

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Entire : gamma-tubulin ring complex

EntireName: gamma-tubulin ring complex
Components
  • Complex: gamma-tubulin ring complex
    • Protein or peptide: Gamma-tubulin complex component 3
    • Protein or peptide: Mitotic-spindle organizing protein 1
    • Protein or peptide: Gamma-tubulin complex component 6
    • Protein or peptide: Actin, cytoplasmic 2, N-terminally processed
    • Protein or peptide: Gamma-tubulin complex component 2
    • Protein or peptide: Ubiquitin-like protein SMT3,CDK5 regulatory subunit-associated protein 2,Microtubule-associated protein RP/EB family member 1
    • Protein or peptide: Isoform 1 of Tubulin alpha-1B chain
    • Protein or peptide: Tubulin beta-3 chain
    • Protein or peptide: Mitotic-spindle organizing protein 2A
    • Protein or peptide: Gamma-tubulin complex component 4
    • Protein or peptide: Gamma-tubulin complex component 5
    • Protein or peptide: Tubulin gamma-1 chain
  • Ligand: GUANOSINE-5'-TRIPHOSPHATE

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Supramolecule #1: gamma-tubulin ring complex

SupramoleculeName: gamma-tubulin ring complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#12
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Gamma-tubulin complex component 3

MacromoleculeName: Gamma-tubulin complex component 3 / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 103.710102 KDa
SequenceString: MATPDQKSPN VLLQNLCCRI LGRSEADVAQ QFQYAVRVIG SNFAPTVERD EFLVAEKIKK ELIRQRREAD AALFSELHRK LHSQGVLKN KWSILYLLLS LSEDPRRQPS KVSSYATLFA QALPRDAHST PYYYARPQTL PLSYQDRSAQ SAQSSGSVGS S GISSIGLC ...String:
MATPDQKSPN VLLQNLCCRI LGRSEADVAQ QFQYAVRVIG SNFAPTVERD EFLVAEKIKK ELIRQRREAD AALFSELHRK LHSQGVLKN KWSILYLLLS LSEDPRRQPS KVSSYATLFA QALPRDAHST PYYYARPQTL PLSYQDRSAQ SAQSSGSVGS S GISSIGLC ALSGPAPAPQ SLLPGQSNQA PGVGDCLRQQ LGSRLAWTLT ANQPSSQATT SKGVPSAVSR NMTRSRREGD TG GTMEITE AALVRDILYV FQGIDGKNIK MNNTENCYKV EGKANLSRSL RDTAVRLSEL GWLHNKIRRY TDQRSLDRSF GLV GQSFCA ALHQELREYY RLLSVLHSQL QLEDDQGVNL GLESSLTLRR LLVWTYDPKI RLKTLAALVD HCQGRKGGEL ASAV HAYTK TGDPYMRSLV QHILSLVSHP VLSFLYRWIY DGELEDTYHE FFVASDPTVK TDRLWHDKYT LRKSMIPSFM TMDQS RKVL LIGKSINFLH QVCHDQTPTT KMIAVTKSAE SPQDAADLFT DLENAFQGKI DAAYFETSKY LLDVLNKKYS LLDHMQ AMR RYLLLGQGDF IRHLMDLLKP ELVRPATTLY QHNLTGILET AVRATNAQFD SPEILRRLDV RLLEVSPGDT GWDVFSL DY HVDGPIATVF TRECMSHYLR VFNFLWRAKR MEYILTDIRK GHMCNAKLLR NMPEFSGVLH QCHILASEMV HFIHQMQY Y ITFEVLECSW DELWNKVQQA QDLDHIIAAH EVFLDTIISR CLLDSDSRAL LNQLRAVFDQ IIELQNAQDA IYRAALEEL QRRLQFEEKK KQREIEGQWG VTAAEEEEEN KRIGEFKESI PKMCSQLRIL THFYQGIVQQ FLVLLTTSSD ESLRFLSFRL DFNEHYKAR EPRLRVSLGT RGRRSSHT

UniProtKB: Gamma-tubulin complex component 3

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Macromolecule #2: Mitotic-spindle organizing protein 1

MacromoleculeName: Mitotic-spindle organizing protein 1 / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 8.485724 KDa
SequenceString:
MASSSGAGAA AAAAAANLNA VRETMDVLLE ISRILNTGLD METLSICVRL CEQGINPEAL SSVIKELRKA TEALKAAENM TS

UniProtKB: Mitotic-spindle organizing protein 1

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Macromolecule #3: Gamma-tubulin complex component 6

MacromoleculeName: Gamma-tubulin complex component 6 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 200.733641 KDa
SequenceString: MASITQLFDD LCEALLPAAK THLGQRSVNR KRAKRSLKKV AYNALFTNLF QDETQQLQPD MSKLPARNKI LMLSFDLRVG GLGPKADRL EELVEELEAA PCCPLLEVGS VLDLLVQLAG SGPPQVLPRK RDYFLNNKHV GRNVPYSGYD CDDLSVFEMD V QSLISREE ...String:
MASITQLFDD LCEALLPAAK THLGQRSVNR KRAKRSLKKV AYNALFTNLF QDETQQLQPD MSKLPARNKI LMLSFDLRVG GLGPKADRL EELVEELEAA PCCPLLEVGS VLDLLVQLAG SGPPQVLPRK RDYFLNNKHV GRNVPYSGYD CDDLSVFEMD V QSLISREE CLCHSMIQET LQVMEAAPGT GLPTVGLFSF GDPCGDRFER DTRVSLFGAL VHSRTYDMDV RLGLPPVPDN AD LSGLAIK VPPSVDQWED EGFQSASNLT PDSQSEPSVT PDVDLWEAAL TYEASKRRCW ERVGCPPGHR EEPYLTEAGR DAF DKFCRL HQGELQLLAG GVLQAPQPVL VKECELVKDV LNVLIGVVSA TFSLCQPAQA FVVKRGVHVS GASPESISSL LSEV AEYGT CYTRLSHFSL QPVLDSLYSK GLVFQAFTSG LRRYLQYYRA CVLSTPPTLS LLTIGFLFKK LGRQLRYLAE LCGVG AVLP GTCGGGPRAA FPTGVKLLSY LYQEALHNCS NEHYPVLLSL LKTSCEPYTR FIHDWVYSGV FRDAYGEFMI QVNHEY LSF RDKLYWTHGY VLISKEVEDC VPVFLKHIAH DIYVCGKTIN LLKLCCPRHY LCWSDVPVPR ISVIFSLEEL KEIEKDC AV YVGRMERVAR HSSVSKEEKE LRMEIAKQEL IAHAREAASR VLSALSDRQM SERMALDARK REQFQRLKEQ FVKDQERR Q AARQEELDDD FSYARELRDR ERRLKSLEEE LERKARQALV DHYSKLSAEA ARREQKALWR IQRHRLESAR LRFLLEDEK HIQEMLKAVS EAHQPQEPPD VLLSVHPQVT SPGPEHPEGG QGCDSGSAEQ HSPAWDGWNR PGLLTPQPLK PLAVGAGGRG LQQAEGARP FSDSLSIGDF LPVGPGAEPS VQTGMVPLLE VALQTINLDL PPSAPGEAPA AASTQPSRPQ EYDFSTVLRP A VATSPAPG PLQAAECSLG SSGLQLWEDS CGKMDACGSA SRETLLPSHP PRRAALEEGS SQPTERLFGQ VSGGGLPTGD YA SEIAPTR PRWNTHGHVS DASIRVGENV SDVAPTQPRW NTHGHVSNAS ISLGESVSDV APTRPRWNIH GHVSNASIRV GEN VSDVAP TRPRWNTHGH VSNASIRVGE NVSDVAPTRP RWNTHGHVSD ASISLGESVS DMAPARPRWN THGHVSDASI SLGE SVSDM APTRPRWNTH GHVSDTSIRV GENVSDVAPI RSRCNTHGHV SDASISLGEP VSDVVSTRPR WNTHVPIPPP HMVLG ALSP EAEPNTPRPQ QSPPGHTSQS ALSLGAQSTV LDCGPRLPVE VGPSLSSPSS GCGEGSISVG ENVSDVAPTQ PWWPNT PGD SVSEELGPGR SGDTEDLSPN WPLNSQEDTA AQSSPGRGEE AEASAAEAQG GEQAYLAGLA GQYHLERYPD SYESMSE PP IAHLLRPVLP RAFAFPVDPQ VQSAADETAV QLSELLTLPV LMKRSITAPL AAHISLVNKA AVDYFFVELH LEAHYEAL R HFLLMEDGEF AQSLSDLLFE KLGAGQTPGE LLNPLVLNSV LSKALQCSLH GDTPHASNLS LALKYLPEVF APNAPDVLS CLELRYKVDW PLNIVITEGC VSKYSGVFSF LLQLKLMMWA LKDVCFHLKR TALLSHMAGS VQFRQLQLFK HEMQHFVKVI QGYIANQIL HVTWCEFRAR LATVGDLEEI QRAHAEYLHK AVFRGLLTEK AAPVMNVIHS IFSLVLKFRS QLISQAWGPP G GPRGAEHP NFALMQQSYN TFKYYSHFLF KVVTKLVNRG YQPHLEDFLL RINFNNYYQD A

UniProtKB: Gamma-tubulin complex component 6

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Macromolecule #4: Actin, cytoplasmic 2, N-terminally processed

MacromoleculeName: Actin, cytoplasmic 2, N-terminally processed / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 41.723527 KDa
SequenceString: DEEVAALVVD NGSGMCKAGF AGDDAPRAVF PSIVGRPRHQ GVMVGMGQKD SYVGDEAQSK RGILTLKYPI EHGIVTNWDD MEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVLDSGDGVS H TVPIYEGY ...String:
DEEVAALVVD NGSGMCKAGF AGDDAPRAVF PSIVGRPRHQ GVMVGMGQKD SYVGDEAQSK RGILTLKYPI EHGIVTNWDD MEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVLDSGDGVS H TVPIYEGY ALPHAILRLD LAGRDLTDYL MKILTERGYS FTTTEEREIV RDIKEKLCYV ALDFEQEMAT AASSSSLEKS YE LKDGQVI TIGNERFRCP EALFQPSFLG MEACGIHETT YNSIMKCDVD IRKDLYANTV LSGGTTMYPG IADRMQKEIT ALA PSTMKI KIIAPPERKY SVWIGGSILA SLSTFQQMWI SKQEYDESGP SIVHRKCF

UniProtKB: Actin, cytoplasmic 2

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Macromolecule #5: Gamma-tubulin complex component 2

MacromoleculeName: Gamma-tubulin complex component 2 / type: protein_or_peptide / ID: 5 / Number of copies: 8 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 102.666953 KDa
SequenceString: MSEFRIHHDV NELLSLLRVH GGDGAEVYID LLQKNRTPYV TTTVSAHSAK VKIAEFSRTP EDFLKKYDEL KSKNTRNLDP LVYLLSKLT EDKETLQYLQ QNAKERAELA AAAVGSSTTS INVPAAASKI SMQELEELRK QLGSVATGST LQQSLELKRK M LRDKQNKK ...String:
MSEFRIHHDV NELLSLLRVH GGDGAEVYID LLQKNRTPYV TTTVSAHSAK VKIAEFSRTP EDFLKKYDEL KSKNTRNLDP LVYLLSKLT EDKETLQYLQ QNAKERAELA AAAVGSSTTS INVPAAASKI SMQELEELRK QLGSVATGST LQQSLELKRK M LRDKQNKK NSGQHLPIFP AWVYERPALI GDFLIGAGIS TDTALPIGTL PLASQESAVV EDLLYVLVGV DGRYVSAQPL AG RQSRTFL VDPNLDLSIR ELVHRILPVA ASYSAVTRFI EEKSSFEYGQ VNHALAAAMR TLVKEHLILV SQLEQLHRQG LLS LQKLWF YIQPAMRTMD ILASLATSVD KGECLGGSTL SLLHDRSFSY TGDSQAQELC LYLTKAASAP YFEVLEKWIY RGII HDPYS EFMVEEHELR KERIQEDYND KYWDQRYTIV QQQIPSFLQK MADKILSTGK YLNVVRECGH DVTCPVAKEI IYTLK ERAY VEQIEKAFNY ASKVLLDFLM EEKELVAHLR SIKRYFLMDQ GDFFVHFMDL AEEELRKPVE DITPPRLEAL LELALR MST ANTDPFKDDL KIDLMPHDLI TQLLRVLAIE TKQEKAMAHA DPTELALSGL EAFSFDYIVK WPLSLIINRK ALTRYQM LF RHMFYCKHVE RQLCSVWISN KTAKQHSLHS AQWFAGAFTL RQRMLNFVQN IQYYMMFEVM EPTWHILEKN LKSASNID D VLGHHTGFLD TCLKDCMLTN PELLKVFSKL MSVCVMFTNC MQKFTQSMKL DGELGGQTLE HSTVLGLPAG AEERARKEL ARKHLAEHAD TVQLVSGFEA TINKFDKNFS AHLLDLLARL SIYSTSDCEH GMASVISRLD FNGFYTERLE RLSAERSQKA TPQVPVLRG PPAPAPRVAV TAQ

UniProtKB: Gamma-tubulin complex component 2

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Macromolecule #6: Ubiquitin-like protein SMT3,CDK5 regulatory subunit-associated pr...

MacromoleculeName: Ubiquitin-like protein SMT3,CDK5 regulatory subunit-associated protein 2,Microtubule-associated protein RP/EB family member 1
type: protein_or_peptide / ID: 6 / Number of copies: 9 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 26.765963 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MGSSHHHHHH GSDSEVNQEA KPEVKPEVKP ETHINLKVSD GSSEIFFKIK KTTPLRRLME AFAKRQGKEM DSLRFLYDGI RIQADQTPE DLDMEDNDII EAHREQIGGA WSHPQFEKSA TVSPTRARNM KDFENQITEL KKENFNLKLR IYFLEERMQQ E FHGDDEAA ...String:
MGSSHHHHHH GSDSEVNQEA KPEVKPEVKP ETHINLKVSD GSSEIFFKIK KTTPLRRLME AFAKRQGKEM DSLRFLYDGI RIQADQTPE DLDMEDNDII EAHREQIGGA WSHPQFEKSA TVSPTRARNM KDFENQITEL KKENFNLKLR IYFLEERMQQ E FHGDDEAA ELMQQVNVLK LTVEDLEKER DFYFGKLRNI ELICQENEGE NDPVLQRIVD ILYATDEGFV I

UniProtKB: Small ubiquitin-related modifier, CDK5 regulatory subunit-associated protein 2, Microtubule-associated protein RP/EB family member 1

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Macromolecule #7: Isoform 1 of Tubulin alpha-1B chain

MacromoleculeName: Isoform 1 of Tubulin alpha-1B chain / type: protein_or_peptide / ID: 7 / Number of copies: 11 / Enantiomer: LEVO
EC number: Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 50.190418 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHP EQLITGKEDA ANNYARGHYT IGKEIIDLVL DRIRKLADQC TGLQGFLVFH SFGGGTGSGF TSLLMERLSV D YGKKSKLE ...String:
MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK HVPRAVFVDL EPTVIDEVRT GTYRQLFHP EQLITGKEDA ANNYARGHYT IGKEIIDLVL DRIRKLADQC TGLQGFLVFH SFGGGTGSGF TSLLMERLSV D YGKKSKLE FSIYPAPQVS TAVVEPYNSI LTTHTTLEHS DCAFMVDNEA IYDICRRNLD IERPTYTNLN RLISQIVSSI TA SLRFDGA LNVDLTDFQT NLVPYPRIHF PLATYAPVIS AEKAYHEQLS VAEITNACFE PANQMVKCDP RHGKYMACCL LYR GDVVPK DVNAAIATIK TKRSIQFVDW CPTGFKVGIN YQPPTVVPGG DLAKVQRAVC MLSNTTAIAE AWARLDHKFD LMYA KRAFV HWYVGEGMEE GEFSEAREDM AALEKDYEEV GVDSVEGEGE EEGEEY

UniProtKB: Tubulin alpha-1B chain

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Macromolecule #8: Tubulin beta-3 chain

MacromoleculeName: Tubulin beta-3 chain / type: protein_or_peptide / ID: 8 / Number of copies: 11 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 50.906703 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPSGNYVGDS DLQLERISVY YNEASSHKYV PRAILVDLEP GTMDSVRSGA FGHLFRPDN FIFGQSGAGN NWAKGHYTEG AELVDSVLDV VRKECENCDC LQGFQLTHSL GGGTGSGMGT LLISKVREEY P DRIMNTFS ...String:
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPSGNYVGDS DLQLERISVY YNEASSHKYV PRAILVDLEP GTMDSVRSGA FGHLFRPDN FIFGQSGAGN NWAKGHYTEG AELVDSVLDV VRKECENCDC LQGFQLTHSL GGGTGSGMGT LLISKVREEY P DRIMNTFS VVPSPKVSDT VVEPYNATLS IHQLVENTDE TYCIDNEALY DICFRTLKLA TPTYGDLNHL VSATMSGVTT SL RFPGQLN ADLRKLAVNM VPFPRLHFFM PGFAPLTARG SQQYRALTVP ELTQQMFDAK NMMAACDPRH GRYLTVATVF RGR MSMKEV DEQMLAIQSK NSSYFVEWIP NNVKVAVCDI PPRGLKMSST FIGNSTAIQE LFKRISEQFT AMFRRKAFLH WYTG EGMDE MEFTEAESNM NDLVSEYQQY QDATAEEEGE MYEDDEEESE AQGPK(GDP)

UniProtKB: Tubulin beta-3 chain

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Macromolecule #9: Mitotic-spindle organizing protein 2A

MacromoleculeName: Mitotic-spindle organizing protein 2A / type: protein_or_peptide / ID: 9 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 16.240576 KDa
SequenceString:
MAAQGVGPGP GSAAPPGLEA ARQKLALRRK KVLSTEEMEL YELAQAAGGG IDPDVFKILV DLLKLNVAPL AVFQMLKSMC AGQRLASEP QDPAAVSLPT SSVPETRGRD KGSAALGGVL ALAERSNHEG SSQRMPRQPS ATRLPKGGGP GKSPTQGST

UniProtKB: Mitotic-spindle organizing protein 2A

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Macromolecule #10: Gamma-tubulin complex component 4

MacromoleculeName: Gamma-tubulin complex component 4 / type: protein_or_peptide / ID: 10 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 76.179969 KDa
SequenceString: MIHELLLALS GYPGSIFTWN KRSGLQVSQD FPFLHPSETS VLNRLCRLGT DYIRFTEFIE QYTGHVQQQD HHPSQQGQGG LHGIYLRAF CTGLDSVLQP YRQALLDLEQ EFLGDPHLSI SHVNYFLDQF QLLFPSVMVV VEQIKSQKIH GCQILETVYK H SCGGLPPV ...String:
MIHELLLALS GYPGSIFTWN KRSGLQVSQD FPFLHPSETS VLNRLCRLGT DYIRFTEFIE QYTGHVQQQD HHPSQQGQGG LHGIYLRAF CTGLDSVLQP YRQALLDLEQ EFLGDPHLSI SHVNYFLDQF QLLFPSVMVV VEQIKSQKIH GCQILETVYK H SCGGLPPV RSALEKILAV CHGVMYKQLS AWMLHGLLLD QHEEFFIKQG PSSGNVSAQP EEDEEDLGIG GLTGKQLREL QD LRLIEEE NMLAPSLKQF SLRVEILPSY IPVRVAEKIL FVGESVQMFE NQNVNLTRKG SILKNQEDTF AAELHRLKQQ PLF SLVDFE QVVDRIRSTV AEHLWKLMVE ESDLLGQLKI IKDFYLLGRG ELFQAFIDTA QHMLKTPPTA VTEHDVNVAF QQSA HKVLL DDDNLLPLLH LTIEYHGKEH KADATQAREG PSRETSPREA PASGWAALGL SYKVQWPLHI LFTPAVLEKY NVVFK YLLS VRRVQAELQH CWALQMQRKH LKSNQTDAIK WRLRNHMAFL VDNLQYYLQV DVLESQFSQL LHQINSTRDF ESIRLA HDH FLSNLLAQSF ILLKPVFHCL NEILDLCHSF CSLVSQNLGP LDERGAAQLS ILVKGFSRQS SLLFKILSSV RNHQINS DL AQLLLRLDYN KYYTQAGGTL GSFGM

UniProtKB: Gamma-tubulin complex component 4

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Macromolecule #11: Gamma-tubulin complex component 5

MacromoleculeName: Gamma-tubulin complex component 5 / type: protein_or_peptide / ID: 11 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 118.467547 KDa
SequenceString: MARHGPPWSR LDAQQERDVR ELVRGVAGLQ DEADPNFQLA LNFAWSNFRF HRFLDVNSHK IEKTIEGIYE KFVIHSDLSK AASWKRLTE EFLNAPLPSI KEIKTDAHYS ILSLLLCLSD SPSNSSYVET PRNKEVEKKD DFDWGKYLME DEEMDIGPYM D TPNWSEES ...String:
MARHGPPWSR LDAQQERDVR ELVRGVAGLQ DEADPNFQLA LNFAWSNFRF HRFLDVNSHK IEKTIEGIYE KFVIHSDLSK AASWKRLTE EFLNAPLPSI KEIKTDAHYS ILSLLLCLSD SPSNSSYVET PRNKEVEKKD DFDWGKYLME DEEMDIGPYM D TPNWSEES EEENDQQPLS REDSGIQVDR TPLEEQDQNR KLDPCISWKD EPDDRSWLEH HVVHQYWTAR PSQFPHSLHL HS NLAAVWD QHLYSSDPLY VPDDRVLVTE TQVIRETLWL LSGVKKLFIF QLIDGKVTVR NNIIVTHLTH SCLRSVLEQI AAY GQVVFR LQEFIDEVMG HSSESMLPGS GSVPKKSTEA PFRTYQAFMW ALYKYFISFK EELAEIEKCI INNDTTITLA IVVD KLAPR LSQLKVLHKV FSTGVAEVPP DTRNVVRASH LLNTLYKAIL EYDNVGEASE QTVSLLFSLW VETVRPYLQT VDEWI VHGH LWDGAREFII QRNKNVPVNH RDFWYATYTL YSVSEKTENE EKMSDNASAS SGSDQGPSSR QHTMVSFLKP VLKQII MAG KSMQLLKNLQ CAESTTCQAG ARDAERKSLY TLFLESVQSR LRHGEDSTPQ VLTEQQATKE NLMKMQSIAE SHLELDD VH DPLLAINFAR MYLEQSDFHE KFAGGDVCVD RSSESVTCQT FELTLRSCLY PHIDKQYLDC CGNLMQTLKK DYRLVEYL Q AMRNFFLMEG GDTMYDFYTS IFDKIREKET WQNVSFLNVQ LQEAVGQRYP EDSSRLSISF ENVDTAKKKL PVHILDGLT LSYKVPWPVD IVISLECQKI YNQVFLLLLQ IKWAKYSLDV LLFGELVSTA EKPRLKEGLI HEQDTVAQFG PQKEPVRQQI HRMFLLRVK LMHFVNSLHN YIMTRILHST GLEFQHQVEE AKDLDQLIKI HYRYLSTIHD RCLLREKVSF VKEAIMKVLN L ALMFADGW QAGLGTWRME SIEKMESDFK NCHMFLVTIL NKAVCRGSFP HLESLALSLM AGMEQS

UniProtKB: Gamma-tubulin complex component 5

+
Macromolecule #12: Tubulin gamma-1 chain

MacromoleculeName: Tubulin gamma-1 chain / type: protein_or_peptide / ID: 12 / Number of copies: 14 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 51.22777 KDa
SequenceString: MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY IPRAVLLDLE PRVIHSILNS PYAKLYNPE NIYLSEHGGG AGNNWASGFS QGEKIHEDIF DIIDREADGS DSLEGFVLCH SIAGGTGSGL GSYLLERLND R YPKKLVQT ...String:
MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY IPRAVLLDLE PRVIHSILNS PYAKLYNPE NIYLSEHGGG AGNNWASGFS QGEKIHEDIF DIIDREADGS DSLEGFVLCH SIAGGTGSGL GSYLLERLND R YPKKLVQT YSVFPNQDEM SDVVVQPYNS LLTLKRLTQN ADCVVVLDNT ALNRIATDRL HIQNPSFSQI NQLVSTIMSA ST TTLRYPG YMNNDLIGLI ASLIPTPRLH FLMTGYTPLT TDQSVASVRK TTVLDVMRRL LQPKNVMVST GRDRQTNHCY IAI LNIIQG EVDPTQVHKS LQRIRERKLA NFIPWGPASI QVALSRKSPY LPSAHRVSGL MMANHTSISS LFERTCRQYD KLRK REAFL EQFRKEDMFK DNFDEMDTSR EIVQQLIDEY HAATRPDYIS WGTQEQ

UniProtKB: Tubulin gamma-1 chain

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Macromolecule #13: GUANOSINE-5'-TRIPHOSPHATE

MacromoleculeName: GUANOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 13 / Number of copies: 11 / Formula: GTP
Molecular weightTheoretical: 523.18 Da
Chemical component information

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 6.9
GridModel: Quantifoil R1.2/1.3 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 45 sec. / Pretreatment - Atmosphere: AIR / Details: 15 mA
VitrificationCryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 310 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
SoftwareName: EPU
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 23663 / Average exposure time: 1.3 sec. / Average electron dose: 40.01 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 81000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 1776484
CTF correctionSoftware - Name: CTFFIND (ver. 4) / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL / In silico model: CryoSPARC Ab Initio Reconstruction
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.67 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 5.0) / Number images used: 652699
Initial angle assignmentType: ANGULAR RECONSTITUTION / Software: (Name: cryoSPARC (ver. 4.7.0), RELION (ver. 5.0))
Final angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: RELION (ver. 5.0)
Final 3D classificationDetails: Several 3D classification and heterogeneity analysis methods
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial model
PDB IDChain

7as4

source_name: PDB, initial_model_type: experimental model

6x0u

source_name: PDB, initial_model_type: experimental model
RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-9smx:
CM1-activated gTuRC in complex with nascent alpha-E254D mutant microtubules

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