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Structure of a bacterial ATP synthase

ATP synthases produce ATP from ADP and inorganic phosphate with energy from a transmembrane proton motive force. Bacterial ATP synthases have been studied extensively because they are the simplest form of the enzyme and because of the relative ease of genetic manipulation of these complexes. We expr...

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Detalles Bibliográficos
Autores principales: Guo, Hui, Suzuki, Toshiharu, Rubinstein, John L
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6377231/
https://www.ncbi.nlm.nih.gov/pubmed/30724163
http://dx.doi.org/10.7554/eLife.43128
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author Guo, Hui
Suzuki, Toshiharu
Rubinstein, John L
author_facet Guo, Hui
Suzuki, Toshiharu
Rubinstein, John L
author_sort Guo, Hui
collection PubMed
description ATP synthases produce ATP from ADP and inorganic phosphate with energy from a transmembrane proton motive force. Bacterial ATP synthases have been studied extensively because they are the simplest form of the enzyme and because of the relative ease of genetic manipulation of these complexes. We expressed the Bacillus PS3 ATP synthase in Eschericia coli, purified it, and imaged it by cryo-EM, allowing us to build atomic models of the complex in three rotational states. The position of subunit ε shows how it is able to inhibit ATP hydrolysis while allowing ATP synthesis. The architecture of the membrane region shows how the simple bacterial ATP synthase is able to perform the same core functions as the equivalent, but more complicated, mitochondrial complex. The structures reveal the path of transmembrane proton translocation and provide a model for understanding decades of biochemical analysis interrogating the roles of specific residues in the enzyme.
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spelling pubmed-63772312019-02-20 Structure of a bacterial ATP synthase Guo, Hui Suzuki, Toshiharu Rubinstein, John L eLife Biochemistry and Chemical Biology ATP synthases produce ATP from ADP and inorganic phosphate with energy from a transmembrane proton motive force. Bacterial ATP synthases have been studied extensively because they are the simplest form of the enzyme and because of the relative ease of genetic manipulation of these complexes. We expressed the Bacillus PS3 ATP synthase in Eschericia coli, purified it, and imaged it by cryo-EM, allowing us to build atomic models of the complex in three rotational states. The position of subunit ε shows how it is able to inhibit ATP hydrolysis while allowing ATP synthesis. The architecture of the membrane region shows how the simple bacterial ATP synthase is able to perform the same core functions as the equivalent, but more complicated, mitochondrial complex. The structures reveal the path of transmembrane proton translocation and provide a model for understanding decades of biochemical analysis interrogating the roles of specific residues in the enzyme. eLife Sciences Publications, Ltd 2019-02-06 /pmc/articles/PMC6377231/ /pubmed/30724163 http://dx.doi.org/10.7554/eLife.43128 Text en © 2019, Guo et al http://creativecommons.org/licenses/by/4.0/ http://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited.
spellingShingle Biochemistry and Chemical Biology
Guo, Hui
Suzuki, Toshiharu
Rubinstein, John L
Structure of a bacterial ATP synthase
title Structure of a bacterial ATP synthase
title_full Structure of a bacterial ATP synthase
title_fullStr Structure of a bacterial ATP synthase
title_full_unstemmed Structure of a bacterial ATP synthase
title_short Structure of a bacterial ATP synthase
title_sort structure of a bacterial atp synthase
topic Biochemistry and Chemical Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6377231/
https://www.ncbi.nlm.nih.gov/pubmed/30724163
http://dx.doi.org/10.7554/eLife.43128
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