8HHC

F1 domain of FoF1-ATPase from Bacillus PS3,post-hyd',lowATP

8HHC の概要

• エントリーDOI: 10.2210/pdb8hhc/pdb
• EMDBエントリー: 34760
• 分子名称: ATP synthase subunit alpha, ATP synthase subunit beta, ATP synthase gamma chain, ... (6 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: 7
• 化学式量合計: 358906.80

構造登録者

Nakano, A.,Kishikawa, J.,Mitsuoka, K.,Yokoyama, K. (登録日: 2022-11-16, 公開日: 2023-07-19, 最終更新日: 2025-01-29)

主引用文献

Nakano, A.,Kishikawa, J.I.,Mitsuoka, K.,Yokoyama, K.
Mechanism of ATP hydrolysis dependent rotation of bacterial ATP synthase.
Nat Commun, 14:4090-4090, 2023

PubMed Abstract: F domain of ATP synthase is a rotary ATPase complex in which rotation of central γ-subunit proceeds in 120° steps against a surrounding αβ fueled by ATP hydrolysis. How the ATP hydrolysis reactions occurring in three catalytic αβ dimers are coupled to mechanical rotation is a key outstanding question. Here we describe catalytic intermediates of the F domain in FF synthase from Bacillus PS3 sp. during ATP mediated rotation captured using cryo-EM. The structures reveal that three catalytic events and the first 80° rotation occur simultaneously in F domain when nucleotides are bound at all the three catalytic αβ dimers. The remaining 40° rotation of the complete 120° step is driven by completion of ATP hydrolysis at αβ, and proceeds through three sub-steps (83°, 91°, 101°, and 120°) with three associated conformational intermediates. All sub-steps except for one between 91° and 101° associated with phosphate release, occur independently of the chemical cycle, suggesting that the 40° rotation is largely driven by release of intramolecular strain accumulated by the 80° rotation. Together with our previous results, these findings provide the molecular basis of ATP driven rotation of ATP synthases.

PubMed: 37429854
DOI: 10.1038/s41467-023-39742-5

実験手法

ELECTRON MICROSCOPY (3.3 Å)