6VOI
Chloroplast ATP synthase (O1, CF1)
6VOI の概要
エントリーDOI | 10.2210/pdb6voi/pdb |
EMDBエントリー | 21265 |
分子名称 | ATP synthase subunit alpha, chloroplastic, ATP synthase subunit beta, chloroplastic, ATP synthase delta chain, chloroplastic, ... (7 entities in total) |
機能のキーワード | cf1fo, atp synthase, photosynthesis, translocase |
由来する生物種 | Spinacia oleracea (Spinach) 詳細 |
タンパク質・核酸の鎖数 | 9 |
化学式量合計 | 412906.98 |
構造登録者 | Yang, J.-H.,Williams, D.,Kandiah, E.,Fromme, P.,Chiu, P.-L. (登録日: 2020-01-30, 公開日: 2020-09-09, 最終更新日: 2024-10-16) |
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 Cited by 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: 32879423DOI: 10.1038/s42003-020-01221-8 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (4.03 Å) |
構造検証レポート
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