6VOL

Chloroplast ATP synthase (R2, CF1FO)

Summary for 6VOL

• Entry DOI: 10.2210/pdb6vol/pdb
• EMDB information: 21268
• Descriptor: ATP synthase subunit alpha, chloroplastic, ADENOSINE-5'-TRIPHOSPHATE, ADENOSINE-5'-DIPHOSPHATE, ... (12 entities in total)
• Functional Keywords: cf1fo, atp synthase, photosynthesis, translocase
• Biological source: Spinacia oleracea (Spinach); More
• Total number of polymer chains: 26
• Total formula weight: 598035.98

Authors

Yang, J.-H.,Williams, D.,Kandiah, E.,Fromme, P.,Chiu, P.-L. (deposition date: 2020-01-30, release date: 2020-09-09, Last modification date: 2024-03-06)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (4.06 Å)