1C99
ASP61 DEPROTONATED FORM OF SUBUNIT C OF THE F1FO ATP SYNTHASE OF ESCHERICHIA COLI
Summary for 1C99
| Entry DOI | 10.2210/pdb1c99/pdb |
| Descriptor | PROTEOLIPID F1FO OF ATP SYNTHASE (1 entity in total) |
| Functional Keywords | proteolipid f1fo, atp synthase, proton translocation, proton transport, hydrolase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 8259.06 |
| Authors | Rastogi, V.K.,Girvin, M.E. (deposition date: 1999-04-30, release date: 1999-11-19, Last modification date: 2023-12-27) |
| Primary citation | Rastogi, V.K.,Girvin, M.E. Structural changes linked to proton translocation by subunit c of the ATP synthase. Nature, 402:263-268, 1999 Cited by PubMed Abstract: F1F0 ATP synthases use a transmembrane proton gradient to drive the synthesis of cellular ATP. The structure of the cytosolic F1 portion of the enzyme and the basic mechanism of ATP hydrolysis by F1 are now well established, but how proton translocation through the transmembrane F0 portion drives these catalytic changes is less clear. Here we describe the structural changes in the proton-translocating F0 subunit c that are induced by deprotonating the specific aspartic acid involved in proton transport. Conformational changes between the protonated and deprotonated forms of subunit c provide the structural basis for an explicit mechanism to explain coupling of proton translocation by F0 to the rotation of subunits within the core of F1. Rotation of these subunits within F1 causes the catalytic conformational changes in the active sites of F1 that result in ATP synthesis. PubMed: 10580496DOI: 10.1038/46224 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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