9G3X
Structure of the Partially-assembled gamma-Tubulin Ring Complex from Pig Brain
This is a non-PDB format compatible entry.
Summary for 9G3X
| Entry DOI | 10.2210/pdb9g3x/pdb |
| EMDB information | 51017 |
| Descriptor | Mitotic spindle organizing protein 1, Gamma-tubulin complex component, Gamma-tubulin complex component 3, ... (6 entities in total) |
| Functional Keywords | tubulin complex, structural protein |
| Biological source | Sus scrofa (pig) More |
| Total number of polymer chains | 10 |
| Total formula weight | 625040.62 |
| Authors | Munoz-Hernandez, H.,Wieczorek, M. (deposition date: 2024-07-12, release date: 2024-10-02, Last modification date: 2024-10-09) |
| Primary citation | Xu, Y.,Munoz-Hernandez, H.,Krutyholowa, R.,Marxer, F.,Cetin, F.,Wieczorek, M. Partial closure of the gamma-tubulin ring complex by CDK5RAP2 activates microtubule nucleation. Dev.Cell, 2024 Cited by PubMed 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 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. PubMed: 39321808DOI: 10.1016/j.devcel.2024.09.002 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.5 Å) |
Structure validation
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