5WCB

Katanin hexamer in the ring conformation

5WCB の概要

• エントリーDOI: 10.2210/pdb5wcb/pdb
• 関連するPDBエントリー: 5WC0 5WC1
• EMDBエントリー: 8794 8796
• 分子名称: Meiotic spindle formation protein mei-1, ADENOSINE-5'-TRIPHOSPHATE (2 entities in total)
• 機能のキーワード: microtubule cytoskeleton, microtubule severing protein, aaa atpase, p60, motor protein
• 由来する生物種: Caenorhabditis elegans
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 313350.06

構造登録者

Zehr, E.A.,Szyk, A.,Piszczek, G.,Szczesna, E.,Zuo, X.,Roll-Mecak, A. (登録日: 2017-06-29, 公開日: 2017-08-09, 最終更新日: 2025-05-21)

主引用文献

Zehr, E.,Szyk, A.,Piszczek, G.,Szczesna, E.,Zuo, X.,Roll-Mecak, A.
Katanin spiral and ring structures shed light on power stroke for microtubule severing.
Nat. Struct. Mol. Biol., 24:717-725, 2017

PubMed Abstract: Microtubule-severing enzymes katanin, spastin and fidgetin are AAA ATPases important for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. Because of a lack of known 3D structures for these enzymes, their mechanism of action has remained poorly understood. Here we report the X-ray crystal structure of the monomeric AAA katanin module from Caenorhabditis elegans and cryo-EM reconstructions of the hexamer in two conformations. The structures reveal an unexpected asymmetric arrangement of the AAA domains mediated by structural elements unique to microtubule-severing enzymes and critical for their function. The reconstructions show that katanin cycles between open spiral and closed ring conformations, depending on the ATP occupancy of a gating protomer that tenses or relaxes interprotomer interfaces. Cycling of the hexamer between these conformations would provide the power stroke for microtubule severing.

PubMed: 28783150
DOI: 10.1038/nsmb.3448

実験手法

ELECTRON MICROSCOPY (6 Å)