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| Title | Transition of human γ-tubulin ring complex into a closed conformation during microtubule nucleation. |
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| Journal, issue, pages | Science, Vol. 383, Issue 6685, Page 870-876, Year 2024 |
| Publish date | Feb 23, 2024 |
 Authors | Cláudia Brito / Marina Serna / Pablo Guerra / Oscar Llorca / Thomas Surrey /  |
| PubMed Abstract | Microtubules are essential for intracellular organization and chromosome segregation. They are nucleated by the γ-tubulin ring complex (γTuRC). However, isolated vertebrate γTuRC adopts an open ...Microtubules are essential for intracellular organization and chromosome segregation. They are nucleated by the γ-tubulin ring complex (γTuRC). However, isolated vertebrate γTuRC adopts an open conformation that deviates from the microtubule structure, raising the question of the nucleation mechanism. In this study, we determined cryo-electron microscopy structures of human γTuRC bound to a nascent microtubule. Structural changes of the complex into a closed conformation ensure that γTuRC templates the 13-protofilament microtubules that exist in human cells. Closure is mediated by a latch that interacts with incorporating tubulin, making it part of the closing mechanism. Further rearrangements involve all γTuRC subunits and the removal of the actin-containing luminal bridge. Our proposed mechanism of microtubule nucleation by human γTuRC relies on large-scale structural changes that are likely the target of regulation in cells. |
 External links | Science / PubMed:38305685 |
| Methods | EM (single particle) |
| Resolution | 3.72 - 4.39 Å |
| Structure data | EMDB-18181, PDB-8q62:  EMDB-18182: Closed conformation of the g-tubulin ring complex nucleating microtubules |
| Source |
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 Keywords |  STRUCTURAL PROTEIN / Microtubule / cytoskeleton / g-tubulin ring complex / tubulin |
