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Yorodumi- EMDB-21069: Desnity map of lumenal bridge in reconstruction of the native hum... -
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Basic information
| Entry | Database: EMDB / ID: EMD-21069 | |||||||||
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| Title | Desnity map of lumenal bridge in reconstruction of the native human gamma-tubulin ring complex | |||||||||
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Sample |
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| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||
Authors | Wieczorek M / Urnavicius L / Ti S / Molloy KR / Chait BT / Kapoor TM | |||||||||
| Funding support | United States, 2 items
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Citation | Journal: Cell / Year: 2020Title: 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. | |||||||||
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Structure visualization
| Movie |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_21069.map.gz | 5 MB | EMDB map data format | |
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| Header (meta data) | emd-21069-v30.xml emd-21069.xml | 8.1 KB 8.1 KB | Display Display | EMDB header |
| Images | emd_21069.png | 54.2 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-21069 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-21069 | HTTPS FTP |
-Validation report
| Summary document | emd_21069_validation.pdf.gz | 78.2 KB | Display | EMDB validaton report |
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| Full document | emd_21069_full_validation.pdf.gz | 77.3 KB | Display | |
| Data in XML | emd_21069_validation.xml.gz | 494 B | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-21069 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-21069 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_21069.map.gz / Format: CCP4 / Size: 190.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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
| Entire | Name: Native human gamma-tubulin ring complex |
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| Components |
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-Supramolecule #1: Native human gamma-tubulin ring complex
| Supramolecule | Name: Native human gamma-tubulin ring complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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| Source (natural) | Organism: Homo sapiens (human) |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | 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: FIELD EMISSION GUN |
| 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: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 307228 |
| Initial angle assignment | Type: OTHER / Details: Relion 3.0 |
| Final angle assignment | Type: OTHER / Details: Relion 3.0 |
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About Yorodumi


Homo sapiens (human)
Authors
United States, 2 items
Citation
UCSF Chimera


















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