Structure of a bacterial ATP synthase

Abstract
Data availability
Article and author information
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Abstract

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 e 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.

Data availability

CryoEM maps have been deposited in EMDB and atomic models in PDB.

The following data sets were generated

1. Guo H
2. Rubinstein JL
(2018) Intact class 1
Electron Microscopy Data Bank, EMD-9333.

http://www.ebi.ac.uk/pdbe/entry/emdb/EMD-9333
1. Guo H
2. Rubinstein JL
(2018) Intact class 1
Protein Data Bank, 6N2Y.

http://www.rcsb.org/structure/6N2Y
1. Guo H
2. Rubinstein JL
(2018) Intact class 2
Electron Microscopy Data Bank, EMD-9334.

http://www.ebi.ac.uk/pdbe/entry/emdb/EMD-9334
1. Guo H
2. Rubinstein JL
(2018) Intact class 2
Protein Data Bank, 6N2Z.

http://www.rcsb.org/structure/6N2Z
1. Guo H
2. Rubinstein JL
(2018) Intact class 3
Electron Microscopy Data Bank, EMD-9335.

http://www.ebi.ac.uk/pdbe/entry/emdb/EMD-9335
1. Guo H
2. Rubinstein JL
(2018) Intact class 3
Protein Data Bank, 6N30.

http://www.rcsb.org/structure/6N30
1. Guo H
2. Rubinstein JL
(2018) Focused Fo/stalk class 1
Electron Microscopy Data Bank, EMD-9336.

http://www.ebi.ac.uk/pdbe/entry/emdb/EMD-9336
1. Guo H
2. Rubinstein JL
(2018) Focused Fo/stalk class 2
Electron Microscopy Data Bank, EMD-9337.

http://www.ebi.ac.uk/pdbe/entry/emdb/EMD-9337
1. Guo H
2. Rubinstein JL
(2018) Focused Fo/stalk class 3
Electron Microscopy Data Bank, EMD-9338.

http://www.ebi.ac.uk/pdbe/entry/emdb/EMD-9338
1. Guo H
2. Rubinstein JL
(2018) Focused Fo
Protein Data Bank, 6N2D.

http://www.rcsb.org/structure/6N2D
1. Guo H
2. Rubinstein JL
(2018) Focused Fo
Electron Microscopy Data Bank, EMD-9327.

http://www.ebi.ac.uk/pdbe/entry/emdb/EMD-9327

Article and author information

Author details

Hui Guo

Molecular Medicine, The Hospital for Sick Children, Toronto, Canada

Competing interests
The authors declare that no competing interests exist.
Toshiharu Suzuki

Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Tokyo, Japan

Competing interests
The authors declare that no competing interests exist.
John L Rubinstein

Molecular Medicine, The Hospital for Sick Children, Toronto, Canada

For correspondence
john.rubinstein@utoronto.ca

Competing interests
The authors declare that no competing interests exist.

"This ORCID iD identifies the author of this article:" 0000-0003-0566-2209

Funding

Canadian Institutes of Health Research (MOP 81294)

John L Rubinstein

Canada Research Chairs

John L Rubinstein

Japan Society for the Promotion of Science (JP18H02409)

Toshiharu Suzuki

Canada Foundation for Innovation

John L Rubinstein

The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.

Copyright

This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.