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- Title
Structure of the mitochondrial ATP synthase by electron cryomicroscopy.
- Authors
John L. Rubinstein; John E. Walker; Richard Henderson
- Abstract
We have determined the structure of intact ATP synthase from bovine heart mitochondria by electron cryomicroscopy of single particles. Docking of an atomic model of the F<inf>1</inf>-c<inf>10</inf> subcomplex into a major segment of the map has allowed the 32 Å resolution density to be interpreted as the F<inf>1</inf>-ATPase, a central and a peripheral stalk and an F<inf>O</inf> membrane region that is composed of two domains. One domain of F<inf>O</inf> corresponds to the ring of c-subunits, and the other probably contains the a-subunit, the transmembrane portion of the b-subunit and the remaining integral membrane proteins of F<inf>O</inf>. The peripheral stalk wraps around the molecule and connects the apex of F<inf>1</inf> to the second domain of F<inf>O</inf>. The interaction of the peripheral stalk with F<inf>1</inf>-c<inf>10</inf> implies that it binds to a non-catalytic α-β interface in F<inf>1</inf> and its inclination where it is not attached to F<inf>1</inf> suggests that it has a flexible region that can serve as a stator during both ATP synthesis and ATP hydrolysis.
- Publication
EMBO Journal, 2003, Vol 22, Issue 23, p6182
- ISSN
0261-4189
- Publication type
Academic Journal
- DOI
10.1093/emboj/cdg608