7TJS

Yeast ATP synthase F1 region State 1-3catalytic beta_tight closed without exogenous ATP

これはPDB形式変換不可エントリーです。

7TJS の概要

• エントリーDOI: 10.2210/pdb7tjs/pdb
• EMDBエントリー: 25930
• 分子名称: ATP synthase subunit alpha, ATP synthase subunit beta, ATP synthase subunit gamma, ... (7 entities in total)
• 機能のキーワード: f1-atpase, atp synthase, hydrolase, nanomotor, complex
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 351339.24

構造登録者

Guo, H.,Rubinstein, J.L. (登録日: 2022-01-17, 公開日: 2022-04-20, 最終更新日: 2024-02-21)

主引用文献

Guo, H.,Rubinstein, J.L.
Structure of ATP synthase under strain during catalysis.
Nat Commun, 13:2232-2232, 2022

PubMed Abstract: ATP synthases are macromolecular machines consisting of an ATP-hydrolysis-driven F motor and a proton-translocation-driven F motor. The F and F motors oppose each other's action on a shared rotor subcomplex and are held stationary relative to each other by a peripheral stalk. Structures of resting mitochondrial ATP synthases revealed a left-handed curvature of the peripheral stalk even though rotation of the rotor, driven by either ATP hydrolysis in F or proton translocation through F, would apply a right-handed bending force to the stalk. We used cryoEM to image yeast mitochondrial ATP synthase under strain during ATP-hydrolysis-driven rotary catalysis, revealing a large deformation of the peripheral stalk. The structures show how the peripheral stalk opposes the bending force and suggests that during ATP synthesis proton translocation causes accumulation of strain in the stalk, which relaxes by driving the relative rotation of the rotor through six sub-steps within F, leading to catalysis.

PubMed: 35468906
DOI: 10.1038/s41467-022-29893-2

実験手法

ELECTRON MICROSCOPY (3.2 Å)