The cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems
The nucleation of microtubules from αβ-tubulin subunits is mediated by γtubulin complexes, which vary in composition across organisms. Here, authors present the cryo-EM structure of the heterotetrameric γ-tubulin small complex (γ-TuSC) from C. albicans at near-atomic resolution.
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Autores principales: | , , , , , , , |
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Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2020
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Materias: | |
Acceso en línea: | https://doaj.org/article/c3b177b1e448457da20ea32c914c464f |
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Sumario: | The nucleation of microtubules from αβ-tubulin subunits is mediated by γtubulin complexes, which vary in composition across organisms. Here, authors present the cryo-EM structure of the heterotetrameric γ-tubulin small complex (γ-TuSC) from C. albicans at near-atomic resolution. |
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