Atomic model for the dimeric F region of mitochondrial ATP synthase.

TitleAtomic model for the dimeric F region of mitochondrial ATP synthase.
Publication TypeJournal Article
Year of Publication2017
AuthorsGuo, H, Bueler, SA, Rubinstein, JL
Date Published2017 11 17
KeywordsCryoelectron Microscopy, Crystallography, X-Ray, Mitochondria, Mitochondrial Proton-Translocating ATPases, Models, Molecular, Protein Folding, Protein Multimerization, Protein Structure, Secondary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins

Mitochondrial adenosine triphosphate (ATP) synthase produces the majority of ATP in eukaryotic cells, and its dimerization is necessary to create the inner membrane folds, or cristae, characteristic of mitochondria. Proton translocation through the membrane-embedded F region turns the rotor that drives ATP synthesis in the soluble F region. Although crystal structures of the F region have illustrated how this rotation leads to ATP synthesis, understanding how proton translocation produces the rotation has been impeded by the lack of an experimental atomic model for the F region. Using cryo-electron microscopy, we determined the structure of the dimeric F complex from at a resolution of 3.6 angstroms. The structure clarifies how the protons travel through the complex, how the complex dimerizes, and how the dimers bend the membrane to produce cristae.

Alternate JournalScience
Citation Key10.1126/science.aao4815
PubMed ID29074581
PubMed Central IDPMC6402782
Grant ListP41 GM103310 / GM / NIGMS NIH HHS / United States