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-Structure paper
Title | Structural basis of redox modulation on chloroplast ATP synthase. |
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Journal, issue, pages | Commun Biol, Vol. 3, Issue 1, Page 482, Year 2020 |
Publish date | Sep 2, 2020 |
Authors | Jay-How Yang / Dewight Williams / Eaazhisai Kandiah / Petra Fromme / Po-Lin Chiu / |
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 ...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. |
External links | Commun Biol / PubMed:32879423 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.05 - 7.9 Å |
Structure data | EMDB-21235, PDB-6vm1: EMDB-21238, PDB-6vm4: EMDB-21239, PDB-6vmb: EMDB-21240, PDB-6vmd: EMDB-21241, PDB-6vmg: EMDB-21262, PDB-6vof: EMDB-21263, PDB-6vog: EMDB-21264, PDB-6voh: EMDB-21265, PDB-6voi: EMDB-21266, PDB-6voj: EMDB-21267, PDB-6vok: EMDB-21268, PDB-6vol: EMDB-21269, PDB-6vom: EMDB-21270, PDB-6von: EMDB-21271, PDB-6voo: |
Chemicals | ChemComp-ATP: ChemComp-ADP: ChemComp-TTX: |
Source |
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Keywords | PHOTOSYNTHESIS/TRANSLOCASE / CF1FO / ATP synthase / PHOTOSYNTHESIS / PHOTOSYNTHESIS-TRANSLOCASE complex / TRANSLOCASE |