6VMG

Chloroplast ATP synthase (O3, CF1FO)

6VMG の概要

• エントリーDOI: 10.2210/pdb6vmg/pdb
• EMDBエントリー: 21241
• 分子名称: ATP synthase subunit a, chloroplastic, ATP synthase subunit b, chloroplastic, ATP synthase delta chain, chloroplastic, ... (9 entities in total)
• 機能のキーワード: cf1fo, atp synthase, photosynthesis, photosynthesis-translocase complex, photosynthesis/translocase
• 由来する生物種: Spinacia oleracea (Spinach); 詳細
• タンパク質・核酸の鎖数: 26
• 化学式量合計: 594738.36

構造登録者

Yang, J.-H.,Williams, D.,Kandiah, E.,Fromme, P.,Chiu, P.-L. (登録日: 2020-01-27, 公開日: 2020-09-09, 最終更新日: 2024-03-06)

主引用文献

Yang, J.H.,Williams, D.,Kandiah, E.,Fromme, P.,Chiu, P.L.
Structural basis of redox modulation on chloroplast ATP synthase.
Commun Biol, 3:482-482, 2020

PubMed Abstract: In higher plants, chloroplast ATP synthase has a unique redox switch on its γ subunit that modulates enzyme activity to limit ATP hydrolysis at night. To understand the molecular details of the redox modulation, we used single-particle cryo-EM to determine the structures of spinach chloroplast ATP synthase in both reduced and oxidized states. The disulfide linkage of the oxidized γ subunit introduces a torsional constraint to stabilize the two β hairpin structures. Once reduced, free cysteines alleviate this constraint, resulting in a concerted motion of the enzyme complex and a smooth transition between rotary states to facilitate the ATP synthesis. We added an uncompetitive inhibitor, tentoxin, in the reduced sample to limit the flexibility of the enzyme and obtained high-resolution details. Our cryo-EM structures provide mechanistic insight into the redox modulation of the energy regulation activity of chloroplast ATP synthase.

PubMed: 32879423
DOI: 10.1038/s42003-020-01221-8

実験手法

ELECTRON MICROSCOPY (6.46 Å)