6CP5

Monomer yeast ATP synthase Fo reconstituted in nanodisc with inhibitor of oligomycin bound generated from focused refinement.

Summary for 6CP5

• Entry DOI: 10.2210/pdb6cp5/pdb
• EMDB information: 7547
• Descriptor: ATP synthase subunit 9, mitochondrial, ATP synthase protein 8, ATP synthase subunit a, ... (8 entities in total)
• Functional Keywords: atp synthase, biosynthetic protein
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 16
• Total formula weight: 172427.71

Authors

Srivastava, A.P.,Luo, M.,Symersky, J.,Liao, M.F.,Mueller, D.M. (deposition date: 2018-03-13, release date: 2018-04-11, Last modification date: 2024-10-23)

Primary citation

Srivastava, A.P.,Luo, M.,Zhou, W.,Symersky, J.,Bai, D.,Chambers, M.G.,Faraldo-Gomez, J.D.,Liao, M.,Mueller, D.M.
High-resolution cryo-EM analysis of the yeast ATP synthase in a lipid membrane.
Science, 360:-, 2018

PubMed Abstract: Mitochondrial adenosine triphosphate (ATP) synthase comprises a membrane embedded F motor that rotates to drive ATP synthesis in the F 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 c-ring in the direction of ATP synthesis, relative to the structure of isolated F Our cryo-EM structures show how F and F are coupled, give insight into the proton translocation pathway, and show how oligomycin blocks ATP synthesis.

PubMed: 29650704
DOI: 10.1126/science.aas9699

Experimental method

ELECTRON MICROSCOPY (4.2 Å)