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CryoEM Reveals the Complexity and Diversity of ATP Synthases

During respiration, adenosine triphosphate (ATP) synthases harness the electrochemical proton motive force (PMF) generated by the electron transport chain (ETC) to synthesize ATP. These macromolecular machines operate by a remarkable rotary catalytic mechanism that couples transmembrane proton trans...

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Detalles Bibliográficos
Autores principales: Courbon, Gautier M., Rubinstein, John L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9244403/
https://www.ncbi.nlm.nih.gov/pubmed/35783400
http://dx.doi.org/10.3389/fmicb.2022.864006
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author Courbon, Gautier M.
Rubinstein, John L.
author_facet Courbon, Gautier M.
Rubinstein, John L.
author_sort Courbon, Gautier M.
collection PubMed
description During respiration, adenosine triphosphate (ATP) synthases harness the electrochemical proton motive force (PMF) generated by the electron transport chain (ETC) to synthesize ATP. These macromolecular machines operate by a remarkable rotary catalytic mechanism that couples transmembrane proton translocation to rotation of a rotor subcomplex, and rotation to ATP synthesis. Initially, x-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and cross-linking were the only ways to gain insights into the three-dimensional (3D) structures of ATP synthases and, in particular, provided ground-breaking insights into the soluble parts of the complex that explained the catalytic mechanism by which rotation is coupled to ATP synthesis. In contrast, early electron microscopy was limited to studying the overall shape of the assembly. However, advances in electron cryomicroscopy (cryoEM) have allowed determination of high-resolution structures, including the membrane regions of ATP synthases. These studies revealed the high-resolution structures of the remaining ATP synthase subunits and showed how these subunits work together in the intact macromolecular machine. CryoEM continues to uncover the diversity of ATP synthase structures across species and has begun to show how ATP synthases can be targeted by therapies to treat human diseases.
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spelling pubmed-92444032022-07-01 CryoEM Reveals the Complexity and Diversity of ATP Synthases Courbon, Gautier M. Rubinstein, John L. Front Microbiol Microbiology During respiration, adenosine triphosphate (ATP) synthases harness the electrochemical proton motive force (PMF) generated by the electron transport chain (ETC) to synthesize ATP. These macromolecular machines operate by a remarkable rotary catalytic mechanism that couples transmembrane proton translocation to rotation of a rotor subcomplex, and rotation to ATP synthesis. Initially, x-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and cross-linking were the only ways to gain insights into the three-dimensional (3D) structures of ATP synthases and, in particular, provided ground-breaking insights into the soluble parts of the complex that explained the catalytic mechanism by which rotation is coupled to ATP synthesis. In contrast, early electron microscopy was limited to studying the overall shape of the assembly. However, advances in electron cryomicroscopy (cryoEM) have allowed determination of high-resolution structures, including the membrane regions of ATP synthases. These studies revealed the high-resolution structures of the remaining ATP synthase subunits and showed how these subunits work together in the intact macromolecular machine. CryoEM continues to uncover the diversity of ATP synthase structures across species and has begun to show how ATP synthases can be targeted by therapies to treat human diseases. Frontiers Media S.A. 2022-06-16 /pmc/articles/PMC9244403/ /pubmed/35783400 http://dx.doi.org/10.3389/fmicb.2022.864006 Text en Copyright © 2022 Courbon and Rubinstein. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
Courbon, Gautier M.
Rubinstein, John L.
CryoEM Reveals the Complexity and Diversity of ATP Synthases
title CryoEM Reveals the Complexity and Diversity of ATP Synthases
title_full CryoEM Reveals the Complexity and Diversity of ATP Synthases
title_fullStr CryoEM Reveals the Complexity and Diversity of ATP Synthases
title_full_unstemmed CryoEM Reveals the Complexity and Diversity of ATP Synthases
title_short CryoEM Reveals the Complexity and Diversity of ATP Synthases
title_sort cryoem reveals the complexity and diversity of atp synthases
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9244403/
https://www.ncbi.nlm.nih.gov/pubmed/35783400
http://dx.doi.org/10.3389/fmicb.2022.864006
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