6vof
From Proteopedia
Chloroplast ATP synthase (O2, CF1FO)
Structural highlights
FunctionATPF_SPIOL F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). Publication Abstract from PubMedIn 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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