6B8H
Mosaic model of yeast mitochondrial ATP synthase monomer
Summary for 6B8H
| Entry DOI | 10.2210/pdb6b8h/pdb |
| EMDB information | 7036 7067 |
| Descriptor | ATP synthase subunit 9, mitochondrial, ATP synthase subunit K, mitochondrial, ATP synthase subunit alpha, mitochondrial, ... (19 entities in total) |
| Functional Keywords | complex, proton transporter, membrane protein |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Cellular location | Mitochondrion membrane ; Multi- pass membrane protein : P61829 Mitochondrion inner membrane; Single-pass membrane protein: P81451 Mitochondrion inner membrane : P07251 Mitochondrion: P00830 P38077 Q12165 P09457 P05626 P30902 Q06405 Mitochondrion membrane; Single-pass membrane protein: P00856 P81450 Mitochondrion inner membrane; Multi-pass membrane protein: P00854 |
| Total number of polymer chains | 60 |
| Total formula weight | 1176195.12 |
| Authors | Guo, H.,Bueler, S.A.,Rubinstein, J.L. (deposition date: 2017-10-07, release date: 2018-01-17, Last modification date: 2024-10-30) |
| 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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