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Structural basis of redox modulation on chloroplast ATP synthase

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 s...

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Autores principales: Yang, Jay-How, Williams, Dewight, Kandiah, Eaazhisai, Fromme, Petra, Chiu, Po-Lin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7468127/
https://www.ncbi.nlm.nih.gov/pubmed/32879423
http://dx.doi.org/10.1038/s42003-020-01221-8
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author Yang, Jay-How
Williams, Dewight
Kandiah, Eaazhisai
Fromme, Petra
Chiu, Po-Lin
author_facet Yang, Jay-How
Williams, Dewight
Kandiah, Eaazhisai
Fromme, Petra
Chiu, Po-Lin
author_sort Yang, Jay-How
collection PubMed
description 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.
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spelling pubmed-74681272020-09-11 Structural basis of redox modulation on chloroplast ATP synthase Yang, Jay-How Williams, Dewight Kandiah, Eaazhisai Fromme, Petra Chiu, Po-Lin Commun Biol Article 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. Nature Publishing Group UK 2020-09-02 /pmc/articles/PMC7468127/ /pubmed/32879423 http://dx.doi.org/10.1038/s42003-020-01221-8 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Yang, Jay-How
Williams, Dewight
Kandiah, Eaazhisai
Fromme, Petra
Chiu, Po-Lin
Structural basis of redox modulation on chloroplast ATP synthase
title Structural basis of redox modulation on chloroplast ATP synthase
title_full Structural basis of redox modulation on chloroplast ATP synthase
title_fullStr Structural basis of redox modulation on chloroplast ATP synthase
title_full_unstemmed Structural basis of redox modulation on chloroplast ATP synthase
title_short Structural basis of redox modulation on chloroplast ATP synthase
title_sort structural basis of redox modulation on chloroplast atp synthase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7468127/
https://www.ncbi.nlm.nih.gov/pubmed/32879423
http://dx.doi.org/10.1038/s42003-020-01221-8
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