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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-21073 | |||||||||
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Title | Structure of the native human gamma-tubulin ring complex | |||||||||
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![]() | Tubulin / gamma-tubulin / gamma-tubulin ring complex / gTuRC / g-TuRC / GCP / GCP2 / GCP3 / GCP4 / GCP5 / GCP6 / microtubule / microtubule nucleation / single particle cryo-EM structure / STRUCTURAL PROTEIN | |||||||||
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 | single particle reconstruction / cryo EM / Resolution: 4.3 Å | |||||||||
![]() | Wieczorek M / Urnavicius L | |||||||||
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
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 177.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 26.3 KB 26.3 KB | Display Display | ![]() |
Images | ![]() | 56.5 KB | ||
Filedesc metadata | ![]() | 9.4 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 576.8 KB | Display | ![]() |
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Full document | ![]() | 576.4 KB | Display | |
Data in XML | ![]() | 6.8 KB | Display | |
Data in CIF | ![]() | 7.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6v6sMC ![]() 6v5vC ![]() 6v69C ![]() 6v6bC ![]() 6v6cC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 1.335 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
+Entire : Native human gamma-tubulin ring complex
+Supramolecule #1: Native human gamma-tubulin ring complex
+Macromolecule #1: Gamma-tubulin complex component 2
+Macromolecule #2: Gamma-tubulin complex component 3
+Macromolecule #3: Gamma-tubulin complex component 4
+Macromolecule #4: Gamma-tubulin complex component 5
+Macromolecule #5: Gamma-tubulin complex component 6
+Macromolecule #6: Unassigned poly-alanine chain ("staple")
+Macromolecule #7: beta actin
+Macromolecule #8: Unassigned poly-alanine model ("CC")
+Macromolecule #9: Unassigned poly-alanine model ("HB")
+Macromolecule #10: Unassigned poly-alanine model ("Lumenal bridge helical bundles")
+Macromolecule #11: Tubulin gamma-1 chain
+Macromolecule #12: ADENOSINE-5'-DIPHOSPHATE
+Macromolecule #13: GUANOSINE-5'-DIPHOSPHATE
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 45.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: OTHER / Details: Relion 3.0 initial model generation |
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Final reconstruction | Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 4.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 103172 |
Initial angle assignment | Type: OTHER / Details: Relion 3.0 |
Final angle assignment | Type: OTHER / Details: Relion 3.0 |