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Structural basis of redox modulation on chloroplast ATP synthase (reduced form)


ABSTRACT:

SUBMITTER: Po-Lin Chiu 

PROVIDER: EMPIAR-10475 | biostudies-other |

REPOSITORIES: biostudies-other

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Structural basis of redox modulation on chloroplast ATP synthase.

Yang Jay-How JH   Williams Dewight D   Kandiah Eaazhisai E   Fromme Petra P   Chiu Po-Lin PL  

Communications biology 20200902 1


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 a  ...[more]

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