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| Title | Ring closure activates yeast γTuRC for species-specific microtubule nucleation. |
|---|---|
| Journal, issue, pages | Nat Struct Mol Biol, Vol. 22, Issue 2, Page 132-137, Year 2015 |
| Publish date | Jan 19, 2015 |
 Authors | Justin M Kollman / Charles H Greenberg / Sam Li / Michelle Moritz / Alex Zelter / Kimberly K Fong / Jose-Jesus Fernandez / Andrej Sali / John Kilmartin / Trisha N Davis / David A Agard /    |
| PubMed Abstract | The γ-tubulin ring complex (γTuRC) is the primary microtubule nucleator in cells. γTuRC is assembled from repeating γ-tubulin small complex (γTuSC) subunits and is thought to function as a ...The γ-tubulin ring complex (γTuRC) is the primary microtubule nucleator in cells. γTuRC is assembled from repeating γ-tubulin small complex (γTuSC) subunits and is thought to function as a template by presenting a γ-tubulin ring that mimics microtubule geometry. However, a previous yeast γTuRC structure showed γTuSC in an open conformation that prevents matching to microtubule symmetry. By contrast, we show here that γ-tubulin complexes are in a closed conformation when attached to microtubules. To confirm the functional importance of the closed γTuSC ring, we trapped the closed state and determined its structure, showing that the γ-tubulin ring precisely matches microtubule symmetry and providing detailed insight into γTuRC architecture. Importantly, the closed state is a stronger nucleator, thus suggesting that this conformational switch may allosterically control γTuRC activity. Finally, we demonstrate that γTuRCs have a strong preference for tubulin from the same species. |
 External links | Nat Struct Mol Biol / PubMed:25599398 / PubMed Central |
| Methods | EM (helical sym.) / EM (subtomogram averaging) |
| Resolution | 6.9 - 38.0 Å |
| Structure data |  EMDB-2799:  EMDB-5989: |
| Source |
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Saccharomyces cerevisiae (brewer's yeast)