9G3X

Structure of the Partially-assembled gamma-Tubulin Ring Complex from Pig Brain

これはPDB形式変換不可エントリーです。

9G3X の概要

• エントリーDOI: 10.2210/pdb9g3x/pdb
• EMDBエントリー: 51017
• 分子名称: Mitotic spindle organizing protein 1, Gamma-tubulin complex component, Gamma-tubulin complex component 3, ... (6 entities in total)
• 機能のキーワード: tubulin complex, structural protein
• 由来する生物種: Sus scrofa (pig); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 625040.62

構造登録者

Munoz-Hernandez, H.,Wieczorek, M. (登録日: 2024-07-12, 公開日: 2024-10-02, 最終更新日: 2024-10-09)

主引用文献

Xu, Y.,Munoz-Hernandez, H.,Krutyholowa, R.,Marxer, F.,Cetin, F.,Wieczorek, M.
Partial closure of the gamma-tubulin ring complex by CDK5RAP2 activates microtubule nucleation.
Dev.Cell, 2024

PubMed Abstract: Microtubule nucleation is templated by the γ-tubulin ring complex (γ-TuRC), but its structure deviates from the geometry of α-/β-tubulin in the microtubule, explaining the complex's poor nucleating activity. Several proteins may activate the γ-TuRC, but the mechanisms underlying activation are not known. Here, we determined the structure of the porcine γ-TuRC purified using CDK5RAP2's centrosomin motif 1 (CM1). We identified an unexpected conformation of the γ-TuRC bound to multiple protein modules containing MZT2, GCP2, and CDK5RAP2, resulting in a long-range constriction of the γ-tubulin ring that brings it in closer agreement with the 13-protofilament microtubule. Additional CDK5RAP2 promoted γ-TuRC decoration and stimulated the microtubule-nucleating activities of the porcine γ-TuRC and a reconstituted, CM1-free human complex in single-molecule assays. Our results provide a structural mechanism for the control of microtubule nucleation by CM1 proteins and identify conformational transitions in the γ-TuRC that prime it for microtubule nucleation.

PubMed: 39321808
DOI: 10.1016/j.devcel.2024.09.002

実験手法

ELECTRON MICROSCOPY (4.5 Å)