7QJ6
Structure of recombinant human gamma-Tubulin Ring Complex 10-spoked assembly intermediate (spokes 3-12, substoichiometric spokes 13-14)
Summary for 7QJ6
| Entry DOI | 10.2210/pdb7qj6/pdb |
| EMDB information | 14011 |
| Descriptor | actin, cytoplasmic 1, Mitotic-spindle organizing protein 1, Gamma-tubulin complex component 3, ... (9 entities in total) |
| Functional Keywords | assembly, intermediate, complex, cytosolic protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 31 |
| Total formula weight | 2317512.76 |
| Authors | Zupa, E.,Pfeffer, S. (deposition date: 2021-12-16, release date: 2022-01-26, Last modification date: 2024-07-17) |
| Primary citation | Wurtz, M.,Zupa, E.,Atorino, E.S.,Neuner, A.,Bohler, A.,Rahadian, A.S.,Vermeulen, B.J.A.,Tonon, G.,Eustermann, S.,Schiebel, E.,Pfeffer, S. Modular assembly of the principal microtubule nucleator gamma-TuRC. Nat Commun, 13:473-473, 2022 Cited by PubMed Abstract: The gamma-tubulin ring complex (γ-TuRC) is the principal microtubule nucleation template in vertebrates. Recent cryo-EM reconstructions visualized the intricate quaternary structure of the γ-TuRC, containing more than thirty subunits, raising fundamental questions about γ-TuRC assembly and the role of actin as an integral part of the complex. Here, we reveal the structural mechanism underlying modular γ-TuRC assembly and identify a functional role of actin in microtubule nucleation. During γ-TuRC assembly, a GCP6-stabilized core comprising GCP2-3-4-5-4-6 is expanded by stepwise recruitment, selective stabilization and conformational locking of four pre-formed GCP2-GCP3 units. Formation of the lumenal bridge specifies incorporation of the terminal GCP2-GCP3 unit and thereby leads to closure of the γ-TuRC ring in a left-handed spiral configuration. Actin incorporation into the complex is not relevant for γ-TuRC assembly and structural integrity, but determines γ-TuRC geometry and is required for efficient microtubule nucleation and mitotic chromosome alignment in vivo. PubMed: 35078983DOI: 10.1038/s41467-022-28079-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7.8 Å) |
Structure validation
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