6B2Z
Cryo-EM structure of the dimeric FO region of yeast mitochondrial ATP synthase
Summary for 6B2Z
| Entry DOI | 10.2210/pdb6b2z/pdb |
| Related | 6B2Z 6B8H |
| EMDB information | 7036 7037 7067 |
| Descriptor | ATP synthase subunit c, mitochondrial, ATP synthase subunit k, mitochondrial, ATP synthase protein 8, ... (10 entities in total) |
| Functional Keywords | complex, dimer, mitochondrial inner membrane, proton translocation, membrane protein |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 38 |
| Total formula weight | 384616.64 |
| Authors | Guo, H.,Rubinstein, J.L. (deposition date: 2017-09-20, release date: 2017-11-08, Last modification date: 2025-05-28) |
| Primary citation | Guo, H.,Bueler, S.A.,Rubinstein, J.L. Atomic model for the dimeric FO region of mitochondrial ATP synthase. Science, 358:936-940, 2017 Cited by PubMed Abstract: Mitochondrial adenosine triphosphate (ATP) synthase produces the majority of ATP in eukaryotic cells, and its dimerization is necessary to create the inner membrane folds, or cristae, characteristic of mitochondria. Proton translocation through the membrane-embedded F region turns the rotor that drives ATP synthesis in the soluble F region. Although crystal structures of the F region have illustrated how this rotation leads to ATP synthesis, understanding how proton translocation produces the rotation has been impeded by the lack of an experimental atomic model for the F region. Using cryo-electron microscopy, we determined the structure of the dimeric F complex from at a resolution of 3.6 angstroms. The structure clarifies how the protons travel through the complex, how the complex dimerizes, and how the dimers bend the membrane to produce cristae. PubMed: 29074581DOI: 10.1126/science.aao4815 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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