8AT4

Structure of the augmin holocomplex in closed conformation

8AT4 の概要

• エントリーDOI: 10.2210/pdb8at4/pdb
• EMDBエントリー: 15633
• 分子名称: HAUS augmin-like complex subunit 1, HAUS augmin-like complex subunit 3, HAUS augmin like complex subunit 4 L homeolog, ... (8 entities in total)
• 機能のキーワード: microtubule, branching, nucleation, cell cycle
• 由来する生物種: Xenopus laevis (African clawed frog); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 435934.31

構造登録者

Zupa, E.,Pfeffer, S. (登録日: 2022-08-22, 公開日: 2022-09-28, 最終更新日: 2023-12-13)

主引用文献

Zupa, E.,Wurtz, M.,Neuner, A.,Hoffmann, T.,Rettel, M.,Bohler, A.,Vermeulen, B.J.A.,Eustermann, S.,Schiebel, E.,Pfeffer, S.
The augmin complex architecture reveals structural insights into microtubule branching.
Nat Commun, 13:5635-5635, 2022

PubMed Abstract: In mitosis, the augmin complex binds to spindle microtubules to recruit the γ-tubulin ring complex (γ-TuRC), the principal microtubule nucleator, for the formation of branched microtubules. Our understanding of augmin-mediated microtubule branching is hampered by the lack of structural information on the augmin complex. Here, we elucidate the molecular architecture and conformational plasticity of the augmin complex using an integrative structural biology approach. The elongated structure of the augmin complex is characterised by extensive coiled-coil segments and comprises two structural elements with distinct but complementary functions in γ-TuRC and microtubule binding, linked by a flexible hinge. The augmin complex is recruited to microtubules via a composite microtubule binding site comprising a positively charged unordered extension and two calponin homology domains. Our study provides the structural basis for augmin function in branched microtubule formation, decisively fostering our understanding of spindle formation in mitosis.

PubMed: 36163468
DOI: 10.1038/s41467-022-33228-6

実験手法

ELECTRON MICROSCOPY (33 Å)