Structure of a bacterial ATP synthase.

TitleStructure of a bacterial ATP synthase.
Publication TypeJournal Article
Year of Publication2019
AuthorsGuo, H, Suzuki, T, Rubinstein, JL
JournalElife
Volume8
Date Published2019 Feb 06
ISSN2050-084X
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 PS3 ATP synthase in , 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 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.

DOI10.7554/eLife.43128
Alternate JournalElife
Citation Key10.7554/eLife.43128
PubMed ID30724163
PubMed Central IDPMC6377231
Grant ListMOP 81294 / / Canadian Institutes of Health Research / Canada
JP18H02409 / / Japan Society for the Promotion of Science /