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- EMDB-51018: Structure of the Native CMG-decorated gamma-Tubulin Ring Complex ... -
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Open data
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Basic information
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Title | Structure of the Native CMG-decorated gamma-Tubulin Ring Complex from Pig Brain | |||||||||
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![]() | Tubulin Complex / STRUCTURAL PROTEIN | |||||||||
Function / homology | ![]() Recruitment of mitotic centrosome proteins and complexes / gamma-tubulin complex localization / gamma-tubulin ring complex / polar microtubule / gamma-tubulin complex / microtubule nucleation / gamma-tubulin binding / Recruitment of NuMA to mitotic centrosomes / pericentriolar material / spindle assembly ...Recruitment of mitotic centrosome proteins and complexes / gamma-tubulin complex localization / gamma-tubulin ring complex / polar microtubule / gamma-tubulin complex / microtubule nucleation / gamma-tubulin binding / Recruitment of NuMA to mitotic centrosomes / pericentriolar material / spindle assembly / cytoplasmic microtubule / cytoplasmic microtubule organization / centriole / meiotic cell cycle / spindle microtubule / neuron migration / brain development / microtubule cytoskeleton organization / spindle / spindle pole / cell junction / mitotic cell cycle / microtubule binding / microtubule / calmodulin binding / centrosome / GTP binding / Golgi apparatus / nucleoplasm / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 6.8 Å | |||||||||
![]() | Munoz-Hernandez H / Wieczorek M | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Partial closure of the γ-tubulin ring complex by CDK5RAP2 activates microtubule nucleation. Authors: Yixin Xu / Hugo Muñoz-Hernández / Rościsław Krutyhołowa / Florina Marxer / Ferdane Cetin / Michal Wieczorek / ![]() Abstract: Microtubule nucleation is templated by the γ-tubulin ring complex (γ-TuRC), but its structure deviates from the geometry of α-/β-tubulin in the microtubule, explaining the complex's poor ...Microtubule nucleation is templated by the γ-tubulin ring complex (γ-TuRC), but its structure deviates from the geometry of α-/β-tubulin in the microtubule, explaining the complex's poor nucleating activity. Several proteins may activate the γ-TuRC, but the mechanisms underlying activation are not known. Here, we determined the structure of the porcine γ-TuRC purified using CDK5RAP2's centrosomin motif 1 (CM1). We identified an unexpected conformation of the γ-TuRC bound to multiple protein modules containing MZT2, GCP2, and CDK5RAP2, resulting in a long-range constriction of the γ-tubulin ring that brings it in closer agreement with the 13-protofilament microtubule. Additional CDK5RAP2 promoted γ-TuRC decoration and stimulated the microtubule-nucleating activities of the porcine γ-TuRC and a reconstituted, CM1-free human complex in single-molecule assays. Our results provide a structural mechanism for the control of microtubule nucleation by CM1 proteins and identify conformational transitions in the γ-TuRC that prime it for microtubule nucleation. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 106.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 29 KB 29 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 12.7 KB | Display | ![]() |
Images | ![]() | 58.2 KB | ||
Filedesc metadata | ![]() | 10.5 KB | ||
Others | ![]() ![]() | 200.7 MB 200.7 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 21.7 KB | Display | |
Data in CIF | ![]() | 28.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9g3yMC ![]() 9g3xC ![]() 9g3zC ![]() 9g40C M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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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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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.41333 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_51018_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_51018_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
+Entire : Gamma-Tubulin Ring Complex in native pig brain
+Supramolecule #1: Gamma-Tubulin Ring Complex in native pig brain
+Macromolecule #1: Gamma-tubulin complex component
+Macromolecule #2: Gamma-tubulin complex component 3
+Macromolecule #3: Gamma-tubulin complex component
+Macromolecule #4: Gamma-tubulin complex component
+Macromolecule #5: Tubulin gamma complex associated protein 6
+Macromolecule #6: Mitotic spindle organizing protein 1
+Macromolecule #7: Mitotic-spindle organizing protein 2A isoform X4
+Macromolecule #8: Tubulin gamma chain
+Macromolecule #9: CDK5 regulatory subunit-associated protein 2
-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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Grid | Model: Quantifoil R2/1 / Material: COPPER / Support film - Material: CARBON / Support film - topology: HOLEY |
Vitrification | Cryogen name: ETHANE-PROPANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 55.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.9 µm / Nominal defocus min: 0.9 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |