Summary for 7TMS
| Entry DOI | 10.2210/pdb7tms/pdb |
| EMDB information | 26001 |
| Descriptor | H(+)-transporting two-sector ATPase, V0 assembly protein 1, V-type proton ATPase subunit c'', ... (17 entities in total) |
| Functional Keywords | membrane protein |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Total number of polymer chains | 31 |
| Total formula weight | 989858.11 |
| Authors | Vasanthakumar, T.,Keon, K.A.,Bueler, S.A.,Jaskolka, M.C.,Rubinstein, J.L. (deposition date: 2022-01-20, release date: 2022-04-13, Last modification date: 2025-05-28) |
| Primary citation | Vasanthakumar, T.,Keon, K.A.,Bueler, S.A.,Jaskolka, M.C.,Rubinstein, J.L. Coordinated conformational changes in the V 1 complex during V-ATPase reversible dissociation. Nat.Struct.Mol.Biol., 29:430-439, 2022 Cited by PubMed Abstract: Vacuolar-type ATPases (V-ATPases) are rotary enzymes that acidify intracellular compartments in eukaryotic cells. These multi-subunit complexes consist of a cytoplasmic V region that hydrolyzes ATP and a membrane-embedded V region that transports protons. V-ATPase activity is regulated by reversible dissociation of the two regions, with the isolated V and V complexes becoming autoinhibited on disassembly and subunit C subsequently detaching from V. In yeast, assembly of the V and V regions is mediated by the regulator of the ATPase of vacuoles and endosomes (RAVE) complex through an unknown mechanism. We used cryogenic-electron microscopy of yeast V-ATPase to determine structures of the intact enzyme, the dissociated but complete V complex and the V complex lacking subunit C. On separation, V undergoes a dramatic conformational rearrangement, with its rotational state becoming incompatible for reassembly with V. Loss of subunit C allows V to match the rotational state of V, suggesting how RAVE could reassemble V and V by recruiting subunit C. PubMed: 35469063DOI: 10.1038/s41594-022-00757-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
Download full validation report
