6CP6
Monomer yeast ATP synthase (F1Fo) reconstituted in nanodisc.
Summary for 6CP6
| Entry DOI | 10.2210/pdb6cp6/pdb |
| EMDB information | 7548 |
| Descriptor | ATP synthase subunit 9, mitochondrial, ATP synthase subunit H, mitochondrial, ATP synthase subunit f, mitochondrial, ... (16 entities in total) |
| Functional Keywords | atp synthase, biosynthetic protein |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Total number of polymer chains | 27 |
| Total formula weight | 573364.21 |
| 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: 2024-10-16) |
| 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 Cited by 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: 29650704DOI: 10.1126/science.aas9699 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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