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- Title
Structure of the c<sub>10</sub> ring of the yeast mitochondrial ATP synthase in the open conformation.
- Authors
Symersky, Jindrich; Pagadala, Vijayakanth; Osowski, Daniel; Krah, Alexander; Meier, Thomas; Faraldo-Gómez, José D; Mueller, David M
- Abstract
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 c10 ring from Saccharomyces cerevisiae determined at pH 8.3, 6.1 and 5.5, at resolutions of 2.0 Å, 2.5 Å and 2.0 Å, 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.
- Publication
Nature Structural & Molecular Biology, 2012, Vol 19, Issue 5, p485
- ISSN
1545-9993
- Publication type
Academic Journal
- DOI
10.1038/nsmb.2284