7ANZ
Structure of the Candida albicans gamma-Tubulin Small Complex
7ANZ の概要
| エントリーDOI | 10.2210/pdb7anz/pdb |
| EMDBエントリー | 11835 |
| 分子名称 | Tubulin gamma chain, Spindle pole body component (3 entities in total) |
| 機能のキーワード | gamma-tubulin small complex, cytoskeleton, microtubule nucleation, cytosolic protein |
| 由来する生物種 | Candida albicans 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 307021.72 |
| 構造登録者 | |
| 主引用文献 | Zupa, E.,Zheng, A.,Neuner, A.,Wurtz, M.,Liu, P.,Bohler, A.,Schiebel, E.,Pfeffer, S. The cryo-EM structure of a gamma-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems. Nat Commun, 11:5705-5705, 2020 Cited by PubMed Abstract: The nucleation of microtubules from αβ-tubulin subunits is mediated by γ-tubulin complexes, which vary in composition across organisms. Aiming to understand how de novo microtubule formation is achieved and regulated by a minimal microtubule nucleation system, we here determined the cryo-electron microscopy structure of the heterotetrameric γ-tubulin small complex (γ-TuSC) from C. albicans at near-atomic resolution. Compared to the vertebrate γ-tubulin ring complex (γ-TuRC), we observed a vastly remodeled interface between the SPC/GCP-γ-tubulin spokes, which stabilizes the complex and defines the γ-tubulin arrangement. The relative positioning of γ-tubulin subunits indicates that a conformational rearrangement of the complex is required for microtubule nucleation activity, which follows opposing directionality as predicted for the vertebrate γ-TuRC. Collectively, our data suggest that the assembly and regulation mechanisms of γ-tubulin complexes fundamentally differ between the microtubule nucleation systems in lower and higher eukaryotes. PubMed: 33177498DOI: 10.1038/s41467-020-19456-8 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.6 Å) |
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