%0 Journal Article
%T High-resolution cryo-EM analysis of the yeast ATP synthase in a lipid membrane
%J -
%D 2018
%R 10.1126/science.aas9699
%X Mitochondrial adenosine triphosphate (ATP) synthase comprises a membrane embedded Fo motor that rotates to drive ATP synthesis in the F1 subunit. We used single-particle cryo¨Celectron microscopy (cryo-EM) to obtain structures of the full complex in a lipid bilayer in the absence or presence of the inhibitor oligomycin at 3.6- and 3.8-angstrom resolution, respectively. To limit conformational heterogeneity, we locked the rotor in a single conformation by fusing the F6 subunit of the stator with the ¦Ä subunit of the rotor. Assembly of the enzyme with the F6-¦Ä fusion caused a twisting of the rotor and a 9¡ã rotation of the Fo c10-ring in the direction of ATP synthesis, relative to the structure of isolated Fo. Our cryo-EM structures show how F1 and Fo are coupled, give insight into the proton translocation pathway, and show how oligomycin blocks ATP synthesis
%U http://science.sciencemag.org/content/360/6389/eaas9699