8DBQ

E. coli ATP synthase imaged in 10mM MgATP State1 "half-up" Fo classified

これはPDB形式変換不可エントリーです。

8DBQ の概要

• エントリーDOI: 10.2210/pdb8dbq/pdb
• 関連するPDBエントリー: 8DBP 8DBR 8DBS 8DBT 8DBU 8DBV 8DBW
• EMDBエントリー: 27296 27297 27298 27299 27300 27301 27302 27303 27304 27305 27306 27307 27308 27309 27310 27311 27312 27313 27314 27315
• 分子名称: ATP synthase subunit alpha, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (12 entities in total)
• 機能のキーワード: energy, atp hyrolysis, atp synthesis, motor, membrane protein, cryoem
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 22
• 化学式量合計: 524410.94

構造登録者

Sobti, M.,Stewart, A.G. (登録日: 2022-06-14, 公開日: 2023-01-25, 最終更新日: 2024-06-12)

主引用文献

Sobti, M.,Zeng, Y.C.,Walshe, J.L.,Brown, S.H.J.,Ishmukhametov, R.,Stewart, A.G.
Changes within the central stalk of E. coli F 1 F o ATP synthase observed after addition of ATP.
Commun Biol, 6:26-26, 2023

PubMed Abstract: FF ATP synthase functions as a biological generator and makes a major contribution to cellular energy production. Proton flow generates rotation in the F motor that is transferred to the F motor to catalyze ATP production, with flexible F/F coupling required for efficient catalysis. FF ATP synthase can also operate in reverse, hydrolyzing ATP and pumping protons, and in bacteria this function can be regulated by an inhibitory ε subunit. Here we present cryo-EM data showing E. coli FF ATP synthase in different rotational and inhibited sub-states, observed following incubation with 10 mM MgATP. Our structures demonstrate how structural transitions within the inhibitory ε subunit induce torsional movement in the central stalk, thereby enabling its rotation within the F motor. This highlights the importance of the central rotor for flexible coupling of the F and F motors and provides further insight into the regulatory mechanism mediated by subunit ε.

PubMed: 36631659
DOI: 10.1038/s42003-023-04414-z

実験手法

ELECTRON MICROSCOPY (4 Å)