8VA2
Symmetry expanded map of 2 gamma-tubulins bound to 2 alpha tubulins in gamma tubulin ring complex capped microtubule end.
Summary for 8VA2
| Entry DOI | 10.2210/pdb8va2/pdb |
| EMDB information | 43085 |
| Descriptor | Tubulin alpha-1B chain, Tubulin gamma-1 chain, GUANOSINE-5'-TRIPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | gamma tubulin ring complex, cell cycle |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 204059.04 |
| Authors | Aher, A.,Urnavicius, L.,Kapoor, T.M. (deposition date: 2023-12-10, release date: 2024-03-27, Last modification date: 2024-10-09) |
| Primary citation | Aher, A.,Urnavicius, L.,Xue, A.,Neselu, K.,Kapoor, T.M. Structure of the gamma-tubulin ring complex-capped microtubule. Nat.Struct.Mol.Biol., 31:1124-1133, 2024 Cited by PubMed Abstract: Microtubules are composed of α-tubulin and β-tubulin dimers positioned head-to-tail to form protofilaments that associate laterally in varying numbers. It is not known how cellular microtubules assemble with the canonical 13-protofilament architecture, resulting in micrometer-scale α/β-tubulin tracks for intracellular transport that align with, rather than spiral along, the long axis of the filament. We report that the human ~2.3 MDa γ-tubulin ring complex (γ-TuRC), an essential regulator of microtubule formation that contains 14 γ-tubulins, selectively nucleates 13-protofilament microtubules. Cryogenic electron microscopy reconstructions of γ-TuRC-capped microtubule minus ends reveal the extensive intra-domain and inter-domain motions of γ-TuRC subunits that accommodate luminal bridge components and establish lateral and longitudinal interactions between γ-tubulins and α-tubulins. Our structures suggest that γ-TuRC, an inefficient nucleation template owing to its splayed conformation, can transform into a compacted cap at the microtubule minus end and set the lattice architecture of cellular microtubules. PubMed: 38609661DOI: 10.1038/s41594-024-01264-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.5 Å) |
Structure validation
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