2XOK
Refined structure of yeast F1c10 ATPase complex to 3 A resolution
Summary for 2XOK
| Entry DOI | 10.2210/pdb2xok/pdb |
| Related | 2WPD |
| Descriptor | ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL, ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL, ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL, ... (8 entities in total) |
| Functional Keywords | hydrolase, atp-binding, f(o), f(1), atp synthase, mitochondria, inner membrane, transmembrane |
| Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) More |
| Total number of polymer chains | 19 |
| Total formula weight | 478949.31 |
| Authors | Stock, D.,W Leslie, A.G.,Walker, J.E. (deposition date: 2010-08-18, release date: 2010-09-22, Last modification date: 2023-12-20) |
| Primary citation | Stock, D.,Leslie, A.G.,Walker, J.E. Molecular architecture of the rotary motor in ATP synthase. Science, 286:1700-1705, 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 (3.01 Å) |
Structure validation
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