Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 19, Issue 5, Pages 485-U40Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2284
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Funding
- US National Institutes of Health [R01GM66223]
- German Research Foundation Cluster of Excellence 'Macromolecular Complexes' [EXC115]
- US Department of Energy, Office of Science, Office of Basic Energy Sciences [W-31-109-Eng-38]
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The proton pore of the F1Fo ATP synthase consists of a ring of c subunits, which rotates, driven by downhill proton diffusion across the membrane. An essential carboxylate side chain in each subunit provides a proton-binding site. In all the structures of c-rings reported to date, these sites are in a closed, ion-locked state. Structures are here presented of the c(10) ring from Saccharomyces cerevisiae determined at pH 8.3, 6.1 and 5.5, at resolutions of 2.0 angstrom, 2.5 angstrom and 2.0 angstrom, respectively. The overall structure of this mitochondrial c-ring is similar to known homologs, except that the essential carboxylate, Glu59, adopts an open extended conformation. Molecular dynamics simulations reveal that opening of the essential carboxylate is a consequence of the amphiphilic nature of the crystallization buffer. We propose that this new structure represents the functionally open form of the c subunit, which facilitates proton loading and release.
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