6vog

Chloroplast ATP synthase (O2, CF1)

spinqualitylabelsall models 6vog, resolution 4.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6vog is a 9 chain structure with sequence from Spinacia oleracea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 4.35Å Ligands: ADP, ATP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ATPA_SPIOL Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Publication Abstract from PubMed In higher plants, chloroplast ATP synthase has a unique redox switch on its gamma 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 gamma subunit introduces a torsional constraint to stabilize the two beta 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. Structural basis of redox modulation on chloroplast ATP synthase.,Yang JH, Williams D, Kandiah E, Fromme P, Chiu PL Commun Biol. 2020 Sep 2;3(1):482. doi: 10.1038/s42003-020-01221-8. PMID:32879423 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase 3D structures

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