6OQW

E. coli ATP synthase State 3a

6OQW の概要

• エントリーDOI: 10.2210/pdb6oqw/pdb
• EMDBエントリー: 20172
• 分子名称: ATP synthase subunit delta, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (12 entities in total)
• 機能のキーワード: e coli atp synthase, ion channel, atpase, membrane protein
• 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: 537205.08

構造登録者

Stewart, A.G.,Sobti, M.,Walshe, J.L. (登録日: 2019-04-29, 公開日: 2020-06-24, 最終更新日: 2024-03-20)

主引用文献

Sobti, M.,Walshe, J.L.,Wu, D.,Ishmukhametov, R.,Zeng, Y.C.,Robinson, C.V.,Berry, R.M.,Stewart, A.G.
Cryo-EM structures provide insight into how E. coli F1FoATP synthase accommodates symmetry mismatch.
Nat Commun, 11:2615-2615, 2020

PubMed Abstract: FF ATP synthase functions as a biological rotary generator that makes a major contribution to cellular energy production. It comprises two molecular motors coupled together by a central and a peripheral stalk. Proton flow through the F motor generates rotation of the central stalk, inducing conformational changes in the F motor that catalyzes ATP production. Here we present nine cryo-EM structures of E. coli ATP synthase to 3.1-3.4 Å resolution, in four discrete rotational sub-states, which provide a comprehensive structural model for this widely studied bacterial molecular machine. We observe torsional flexing of the entire complex and a rotational sub-step of F associated with long-range conformational changes that indicates how this flexibility accommodates the mismatch between the 3- and 10-fold symmetries of the F and F motors. We also identify density likely corresponding to lipid molecules that may contribute to the rotor/stator interaction within the F motor.

PubMed: 32457314
DOI: 10.1038/s41467-020-16387-2

実験手法

ELECTRON MICROSCOPY (3.1 Å)