7XKH

Nucleotide-depleted F1 domain of FoF1-ATPase from Bacillus PS3, state1

7XKH の概要

• エントリーDOI: 10.2210/pdb7xkh/pdb
• EMDBエントリー: 33251
• 分子名称: ATP synthase subunit alpha, ATP synthase subunit beta, ATP synthase gamma chain, ... (5 entities in total)
• 機能のキーワード: atp synthase f1 atpase fof1, motor protein
• 由来する生物種: Bacillus sp. PS3; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 371361.08

構造登録者

Nakano, A.,Kishikawa, J.,Nakanishi, A.,Mitsuoka, K.,Yokoyama, K. (登録日: 2022-04-19, 公開日: 2022-09-21, 最終更新日: 2023-10-11)

主引用文献

Nakano, A.,Kishikawa, J.I.,Nakanishi, A.,Mitsuoka, K.,Yokoyama, K.
Structural basis of unisite catalysis of bacterial F 0 F 1 -ATPase.
Pnas Nexus, 1:pgac116-pgac116, 2022

PubMed Abstract: Adenosine triphosphate (ATP) synthases (FF-ATPases) are crucial for all aerobic organisms. F, a water-soluble domain, can catalyze both the synthesis and hydrolysis of ATP with the rotation of the central rotor inside a cylinder made of in three different conformations (referred to as , , and ). In this study, we determined multiple cryo-electron microscopy structures of bacterial FF exposed to different reaction conditions. The structures of nucleotide-depleted FF indicate that the ε subunit directly forces to adopt a closed form independent of the nucleotide binding to . The structure of FF under conditions that permit only a single catalytic subunit per enzyme to bind ATP is referred to as unisite catalysis and reveals that ATP hydrolysis unexpectedly occurs on instead of , where ATP hydrolysis proceeds in the steady-state catalysis of FF. This indicates that the unisite catalysis of bacterial FF significantly differs from the kinetics of steady-state turnover with continuous rotation of the shaft.

PubMed: 36741449
DOI: 10.1093/pnasnexus/pgac116

実験手法

ELECTRON MICROSCOPY (3.1 Å)