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 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 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.06 Å) |
Structure validation
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