1QO1
Molecular Architecture of the Rotary Motor in ATP Synthase from Yeast Mitochondria
Summary for 1QO1
Entry DOI | 10.2210/pdb1qo1/pdb |
Related | 1A91 1AQT 1BMF 1BSH 1BSN 1COW 1EFR 1NBM |
Descriptor | ATP SYNTHASE ALPHA CHAIN, ATP SYNTHASE BETA CHAIN, ATP SYNTHASE GAMMA CHAIN, ... (5 entities in total) |
Functional Keywords | atp synthase, low resolution model, c-alpha only |
Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) More |
Total number of polymer chains | 18 |
Total formula weight | 448851.35 |
Authors | Stock, D.,Leslie, A.G.W.,Walker, J.E. (deposition date: 1999-11-01, release date: 1999-11-04, Last modification date: 2023-12-13) |
Primary citation | Stock, D.,Leslie, A.G.W.,Walker, J.E. Molecular Architecture of the Rotary Motor in ATP Synthase Science, 286:1700-, 1999 Cited by PubMed Abstract: Adenosine triphosphate (ATP) synthase contains a rotary motor involved in biological energy conversion. Its membrane-embedded F0 sector has a rotation generator fueled by the proton-motive force, which provides the energy required for the synthesis of ATP by the F1 domain. An electron density map obtained from crystals of a subcomplex of yeast mitochondrial ATP synthase shows a ring of 10 c subunits. Each c subunit forms an alpha-helical hairpin. The interhelical loops of six to seven of the c subunits are in close contact with the gamma and delta subunits of the central stalk. The extensive contact between the c ring and the stalk suggests that they may rotate as an ensemble during catalysis. PubMed: 10576729DOI: 10.1126/SCIENCE.286.5445.1700 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.9 Å) |
Structure validation
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