High-resolution cryo-EM analysis of the yeast ATP synthase in a lipid membrane.

ABSTRACT: Mitochondrial adenosine triphosphate (ATP) synthase comprises a membrane embedded F_o motor that rotates to drive ATP synthesis in the F₁ subunit. We used single-particle cryo-electron 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 δ subunit of the rotor. Assembly of the enzyme with the F6-δ fusion caused a twisting of the rotor and a 9° rotation of the F_o c₁₀-ring in the direction of ATP synthesis, relative to the structure of isolated F_o Our cryo-EM structures show ho

SUBMITTER: Srivastava AP 

PROVIDER: S-EPMC5948177 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature