6OQW
E. coli ATP synthase State 3a
Summary for 6OQW
| Entry DOI | 10.2210/pdb6oqw/pdb |
| EMDB information | 20172 |
| Descriptor | ATP synthase subunit delta, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (12 entities in total) |
| Functional Keywords | e coli atp synthase, ion channel, atpase, membrane protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 22 |
| Total formula weight | 537205.08 |
| Authors | Stewart, A.G.,Sobti, M.,Walshe, J.L. (deposition date: 2019-04-29, release date: 2020-06-24, Last modification date: 2024-03-20) |
| Primary citation | Sobti, M.,Walshe, J.L.,Wu, D.,Ishmukhametov, R.,Zeng, Y.C.,Robinson, C.V.,Berry, R.M.,Stewart, A.G. Cryo-EM structures provide insight into how E. coli F1FoATP synthase accommodates symmetry mismatch. Nat Commun, 11:2615-2615, 2020 Cited by PubMed Abstract: FF ATP synthase functions as a biological rotary generator that makes a major contribution to cellular energy production. It comprises two molecular motors coupled together by a central and a peripheral stalk. Proton flow through the F motor generates rotation of the central stalk, inducing conformational changes in the F motor that catalyzes ATP production. Here we present nine cryo-EM structures of E. coli ATP synthase to 3.1-3.4 Å resolution, in four discrete rotational sub-states, which provide a comprehensive structural model for this widely studied bacterial molecular machine. We observe torsional flexing of the entire complex and a rotational sub-step of F associated with long-range conformational changes that indicates how this flexibility accommodates the mismatch between the 3- and 10-fold symmetries of the F and F motors. We also identify density likely corresponding to lipid molecules that may contribute to the rotor/stator interaction within the F motor. PubMed: 32457314DOI: 10.1038/s41467-020-16387-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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