Structure of the mitochondrial ATP synthase from <i>Pichia angusta</i> determined by electron cryo-microscopy.

ABSTRACT: The structure of the intact monomeric ATP synthase from the fungus, Pichia angusta, has been solved by electron cryo-microscopy. The structure provides insights into the mechanical coupling of the transmembrane proton motive force across mitochondrial membranes in the synthesis of ATP. This mechanism requires a strong and integral stator, consisting of the catalytic α₃β₃-domain, peripheral stalk, and, in the membrane domain, subunit a and associated supernumerary subunits, kept in contact with the rotor turning at speeds up to 350 Hz. The stator's integrity is ensured by robust attachment of both the oligomycin sensitivity conferral protein (OSCP) to the catalytic domain and the membrane domain of subunit b to subunit a. The ATP8 subunit provides an additional

SUBMITTER: Vinothkumar KR 

PROVIDER: S-EPMC5111644 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature