7VAS

V1EG domain of V/A-ATPase from Thermus thermophilus at low ATP concentration, state1-2

これはPDB形式変換不可エントリーです。

7VAS の概要

• エントリーDOI: 10.2210/pdb7vas/pdb
• EMDBエントリー: 31861
• 分子名称: V-type ATP synthase alpha chain, V-type ATP synthase beta chain, V-type ATP synthase subunit D, ... (9 entities in total)
• 機能のキーワード: rotary atpase, v-type atpase, atp synthase, thermus thermophilus, chemo-mechanical coupling, motor protein
• 由来する生物種: Thermus thermophilus HB8; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 455285.43

構造登録者

Kishikawa, J.,Nakanishi, A.,Nakano, A.,Saeki, S.,Furuta, A.,Kato, T.,Mitsuoka, K.,Yokoyama, K. (登録日: 2021-08-30, 公開日: 2022-07-13, 最終更新日: 2024-06-19)

主引用文献

Kishikawa, J.,Nakanishi, A.,Nakano, A.,Saeki, S.,Furuta, A.,Kato, T.,Mistuoka, K.,Yokoyama, K.
Structural snapshots of V/A-ATPase reveal the rotary catalytic mechanism of rotary ATPases.
Nat Commun, 13:1213-1213, 2022

PubMed Abstract: V/A-ATPase is a motor protein that shares a common rotary catalytic mechanism with FF ATP synthase. When powered by ATP hydrolysis, the V domain rotates the central rotor against the AB hexamer, composed of three catalytic AB dimers adopting different conformations (AB, AB, and AB). Here, we report the atomic models of 18 catalytic intermediates of the V domain of V/A-ATPase under different reaction conditions, determined by single particle cryo-EM. The models reveal that the rotor does not rotate immediately after binding of ATP to the V. Instead, three events proceed simultaneously with the 120˚ rotation of the shaft: hydrolysis of ATP in AB, zipper movement in AB by the binding ATP, and unzipper movement in AB with release of both ADP and Pi. This indicates the unidirectional rotation of V/A-ATPase by a ratchet-like mechanism owing to ATP hydrolysis in AB, rather than the power stroke model proposed previously for F-ATPase.

PubMed: 35260556
DOI: 10.1038/s41467-022-28832-5

実験手法

ELECTRON MICROSCOPY (3 Å)