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- EMDB-21068: Structure of GCP6 in the native human gamma-tubulin ring complex -

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Basic information

Entry
Database: EMDB / ID: EMD-21068
TitleStructure of GCP6 in the native human gamma-tubulin ring complex
Map data
Sample
  • Complex: Native human gamma-tubulin ring complex
    • Protein or peptide: Gamma-tubulin complex component 6
KeywordsGCP / GCP6 / gamma-tubulin ring complex / gTuRC / g-TuRC / microtubule / microtubule nucleation / single particle cryo-EM structure / STRUCTURAL PROTEIN
Function / homology
Function and homology information


equatorial microtubule organizing center / gamma-tubulin ring complex / gamma-tubulin complex / microtubule nucleation / gamma-tubulin binding / spindle assembly / cytoplasmic microtubule organization / Recruitment of mitotic centrosome proteins and complexes / Recruitment of NuMA to mitotic centrosomes / meiotic cell cycle ...equatorial microtubule organizing center / gamma-tubulin ring complex / gamma-tubulin complex / microtubule nucleation / gamma-tubulin binding / spindle assembly / cytoplasmic microtubule organization / Recruitment of mitotic centrosome proteins and complexes / Recruitment of NuMA to mitotic centrosomes / meiotic cell cycle / spindle pole / mitotic cell cycle / microtubule binding / microtubule / centrosome / membrane / cytosol
Similarity search - Function
Gamma-tubulin complex component 6, N-terminal / Gamma-tubulin complex component 6 N-terminus / 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
Similarity search - Domain/homology
Gamma-tubulin complex component 6
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.5 Å
AuthorsWieczorek M / Urnavicius L
Funding support United States, France, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35 GM130234 United States
Human Frontier Science Program (HFSP)LT000025/18-L1 France
CitationJournal: Cell / Year: 2020
Title: Asymmetric Molecular Architecture of the Human γ-Tubulin Ring Complex.
Authors: Michal Wieczorek / Linas Urnavicius / Shih-Chieh Ti / Kelly R Molloy / Brian T Chait / Tarun M Kapoor /
Abstract: The γ-tubulin ring complex (γ-TuRC) is an essential regulator of centrosomal and acentrosomal microtubule formation, yet its structure is not known. Here, we present a cryo-EM reconstruction of the ...The γ-tubulin ring complex (γ-TuRC) is an essential regulator of centrosomal and acentrosomal microtubule formation, yet its structure is not known. Here, we present a cryo-EM reconstruction of the native human γ-TuRC at ∼3.8 Å resolution, revealing an asymmetric, cone-shaped structure. Pseudo-atomic models indicate that GCP4, GCP5, and GCP6 form distinct Y-shaped assemblies that structurally mimic GCP2/GCP3 subcomplexes distal to the γ-TuRC "seam." We also identify an unanticipated structural bridge that includes an actin-like protein and spans the γ-TuRC lumen. Despite its asymmetric architecture, the γ-TuRC arranges γ-tubulins into a helical geometry poised to nucleate microtubules. Diversity in the γ-TuRC subunits introduces large (>100,000 Å) surfaces in the complex that allow for interactions with different regulatory factors. The observed compositional complexity of the γ-TuRC could self-regulate its assembly into a cone-shaped structure to control microtubule formation across diverse contexts, e.g., within biological condensates or alongside existing filaments.
History
DepositionDec 4, 2019-
Header (metadata) releaseDec 18, 2019-
Map releaseJan 1, 2020-
UpdateMar 6, 2024-
Current statusMar 6, 2024Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.0258
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.0258
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6v6c
  • Surface level: 0.0258
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-6v6c
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_21068.png

Downloads & links

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Map

FileDownload / File: emd_21068.map.gz / Format: CCP4 / Size: 190.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.335 Å
Density
Contour LevelBy AUTHOR: 0.0258 / Movie #1: 0.0258
Minimum - Maximum-0.07161597 - 0.107505605
Average (Standard dev.)0.000072169576 (±0.0019843276)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions368368368
Spacing368368368
CellA=B=C: 491.28003 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.3351.3351.335
M x/y/z368368368
origin x/y/z0.0000.0000.000
length x/y/z491.280491.280491.280
α/β/γ90.00090.00090.000
start NX/NY/NZ-51-35-11
NX/NY/NZ11110799
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS368368368
D min/max/mean-0.0720.1080.000

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Supplemental data

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Sample components

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Entire : Native human gamma-tubulin ring complex

EntireName: Native human gamma-tubulin ring complex
Components
  • Complex: Native human gamma-tubulin ring complex
    • Protein or peptide: Gamma-tubulin complex component 6

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Supramolecule #1: Native human gamma-tubulin ring complex

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

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Macromolecule #1: Gamma-tubulin complex component 6

MacromoleculeName: Gamma-tubulin complex component 6 / type: protein_or_peptide / ID: 1
Details: Please note that the full sequence for GCP6 (Uniprot accession number Q96RT7) was much longer than our modeled region, and the alignment failed to capture the domains we built, despite all ...Details: Please note that the full sequence for GCP6 (Uniprot accession number Q96RT7) was much longer than our modeled region, and the alignment failed to capture the domains we built, despite all residues being numbered accordingly in the submitted coordinates. See below for full sequence.
Number of copies: 1 / 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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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 45.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: OTHER / Details: Relion 3.0 initial model generation
Initial angle assignmentType: OTHER / Details: Relion 3.0
Final angle assignmentType: OTHER / Details: Relion 3.0
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 4.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 102613

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