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Open data
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Basic information
Entry | Database: PDB / ID: 6v6s | |||||||||
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Title | Structure of the native human gamma-tubulin ring complex | |||||||||
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![]() | STRUCTURAL PROTEIN / Tubulin / gamma-tubulin / gamma-tubulin ring complex / gTuRC / g-TuRC / GCP / GCP2 / GCP3 / GCP4 / GCP5 / GCP6 / microtubule / microtubule nucleation / single particle cryo-EM structure | |||||||||
Function / homology | ![]() equatorial microtubule organizing center / mitotic spindle microtubule / gamma-tubulin ring complex / microtubule minus-end binding / polar microtubule / gamma-tubulin complex / meiotic spindle organization / microtubule nucleation / gamma-tubulin binding / non-motile cilium ...equatorial microtubule organizing center / mitotic spindle microtubule / gamma-tubulin ring complex / microtubule minus-end binding / polar microtubule / gamma-tubulin complex / meiotic spindle organization / microtubule nucleation / gamma-tubulin binding / non-motile cilium / microtubule organizing center / pericentriolar material / cell leading edge / cytoplasmic microtubule / mitotic sister chromatid segregation / single fertilization / spindle assembly / cytoplasmic microtubule organization / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / centriole / AURKA Activation by TPX2 / mitotic spindle organization / ciliary basal body / meiotic cell cycle / condensed nuclear chromosome / neuron migration / brain development / recycling endosome / structural constituent of cytoskeleton / spindle pole / microtubule cytoskeleton organization / spindle / microtubule cytoskeleton / Regulation of PLK1 Activity at G2/M Transition / apical part of cell / mitotic cell cycle / microtubule binding / protein-containing complex assembly / microtubule / neuron projection / centrosome / GTP binding / structural molecule activity / nucleoplasm / identical protein binding / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.3 Å | |||||||||
![]() | Wieczorek, M. / Urnavicius, L. / Ti, S. / Molloy, K.R. / Chait, B.T. / Kapoor, T.M. | |||||||||
Funding support | ![]() ![]()
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![]() | ![]() 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 |
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 2.4 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2 MB | Display | ![]() |
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Full document | ![]() | 2.1 MB | Display | |
Data in XML | ![]() | 287.1 KB | Display | |
Data in CIF | ![]() | 468.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 21073MC ![]() 6v5vC ![]() 6v69C ![]() 6v6bC ![]() 6v6cC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Components
-Gamma-tubulin complex component ... , 5 types, 14 molecules ACEGMBDFHTIKJL
#1: Protein | Mass: 105765.719 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Protein | Mass: 103710.102 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein | Mass: 76179.969 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | | Mass: 118467.547 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | | Mass: 200733.641 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: Sequence truncated around modeled region of GCP6 to enable deposition; full sequence can be found at Uniprot # Q96RT7. Source: (natural) ![]() |
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-Protein/peptide , 1 types, 5 molecules NOQRS
#6: Protein/peptide | Mass: 4273.259 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Protein , 2 types, 15 molecules Uabcdefghijklmt
#7: Protein | Mass: 41723.527 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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#11: Protein | Mass: 51255.824 Da / Num. of mol.: 14 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Unassigned poly-alanine model ... , 3 types, 4 molecules VYWX
#8: Protein | Mass: 5634.938 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | | Mass: 14060.317 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein | | Mass: 22400.504 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 2 types, 15 molecules ![](data/chem/img/ADP.gif)
![](data/chem/img/GDP.gif)
![](data/chem/img/GDP.gif)
#12: Chemical | ChemComp-ADP / |
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#13: Chemical | ChemComp-GDP / |
-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: Native human gamma-tubulin ring complex / Type: COMPLEX / Entity ID: #1-#6, #8-#10 / Source: NATURAL |
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Source (natural) | Organism: ![]() |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 45 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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Symmetry | Point symmetry: C1 (asymmetric) |
3D reconstruction | Resolution: 4.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 103172 / Symmetry type: POINT |