6LY8

V/A-ATPase from Thermus thermophilus, the soluble domain, including V1, d, two EG stalks, and N-terminal domain of a-subunit.

6LY8 の概要

• エントリーDOI: 10.2210/pdb6ly8/pdb
• EMDBエントリー: 30014
• 分子名称: V-type ATP synthase alpha chain, V-type ATP synthase beta chain, V-type ATP synthase subunit D, ... (5 entities in total)
• 機能のキーワード: rotary atpase, v/a-atpase, molecular motor, motor protein
• 由来する生物種: Thermus thermophilus HB8; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 387196.11

構造登録者

Kishikawa, J.,Nakanishi, A.,Furuta, A.,Kato, T.,Namba, K.,Tamakoshi, M.,Mitsuoka, K.,Yokoyama, K. (登録日: 2020-02-13, 公開日: 2020-09-09, 最終更新日: 2025-09-17)

主引用文献

Kishikawa, J.I.,Nakanishi, A.,Furuta, A.,Kato, T.,Namba, K.,Tamakoshi, M.,Mitsuoka, K.,Yokoyama, K.
Mechanical inhibition of isolated V o from V/A-ATPase for proton conductance.
Elife, 9:-, 2020

PubMed Abstract: V-ATPase is an energy converting enzyme, coupling ATP hydrolysis/synthesis in the hydrophilic V domain, with proton flow through the V membrane domain, via rotation of the central rotor complex relative to the surrounding stator apparatus. Upon dissociation from the V domain, the V domain of the eukaryotic V-ATPase can adopt a physiologically relevant auto-inhibited form in which proton conductance through the V domain is prevented, however the molecular mechanism of this inhibition is not fully understood. Using cryo-electron microscopy, we determined the structure of both the V/A-ATPase and isolated V at near-atomic resolution, respectively. These structures clarify how the isolated V domain adopts the auto-inhibited form and how the complex prevents formation of the inhibited V form.

PubMed: 32639230
DOI: 10.7554/eLife.56862

実験手法

ELECTRON MICROSCOPY (3.5 Å)