+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-21073 | |||||||||
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Title | Structure of the native human gamma-tubulin ring complex | |||||||||
Map data | ||||||||||
Sample |
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Keywords | 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 | Function and homology information equatorial microtubule organizing center / mitotic spindle microtubule / gamma-tubulin ring complex / polar microtubule / gamma-tubulin complex / meiotic spindle organization / microtubule nucleation / gamma-tubulin binding / non-motile cilium / microtubule organizing center ...equatorial microtubule organizing center / mitotic spindle microtubule / gamma-tubulin ring complex / polar microtubule / gamma-tubulin complex / meiotic spindle organization / microtubule nucleation / gamma-tubulin binding / non-motile cilium / microtubule organizing center / pericentriolar material / cytoplasmic microtubule / cell leading edge / mitotic sister chromatid segregation / condensed nuclear chromosome / single fertilization / spindle assembly / meiotic cell cycle / 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 / 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 | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.3 Å | |||||||||
Authors | Wieczorek M / Urnavicius L | |||||||||
Funding support | United States, France, 2 items
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Citation | Journal: 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 |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_21073.map.gz | 177.6 MB | EMDB map data format | |
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Header (meta data) | emd-21073-v30.xml emd-21073.xml | 26.3 KB 26.3 KB | Display Display | EMDB header |
Images | emd_21073.png | 56.5 KB | ||
Filedesc metadata | emd-21073.cif.gz | 9.4 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-21073 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-21073 | HTTPS FTP |
-Validation report
Summary document | emd_21073_validation.pdf.gz | 576.8 KB | Display | EMDB validaton report |
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Full document | emd_21073_full_validation.pdf.gz | 576.4 KB | Display | |
Data in XML | emd_21073_validation.xml.gz | 6.8 KB | Display | |
Data in CIF | emd_21073_validation.cif.gz | 7.7 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-21073 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-21073 | HTTPS FTP |
-Related structure data
Related structure data | 6v6sMC 6v5vC 6v69C 6v6bC 6v6cC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_21073.map.gz / Format: CCP4 / Size: 190.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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
-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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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
-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: FIELD EMISSION GUN |
Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-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 |