Summary for 9COP
| Entry DOI | 10.2210/pdb9cop/pdb |
| EMDB information | 45788 46463 |
| Descriptor | V-type proton ATPase catalytic subunit A, Suppressor of kinetochore protein 1, MAGNESIUM ION, ... (12 entities in total) |
| Functional Keywords | v-atpase, rave, assembly, hydrolase |
| Biological source | Saccharomyces cerevisiae (brewer's yeast) More |
| Total number of polymer chains | 14 |
| Total formula weight | 747203.59 |
| Authors | Wang, H.,Rubinstein, J.L. (deposition date: 2024-07-17, release date: 2024-11-20, Last modification date: 2025-06-04) |
| Primary citation | Wang, H.,Tarsio, M.,Kane, P.M.,Rubinstein, J.L. Structure of yeast RAVE bound to a partial V 1 complex. Proc.Natl.Acad.Sci.USA, 121:e2414511121-e2414511121, 2024 Cited by PubMed Abstract: Vacuolar-type ATPases (V-ATPases) are membrane-embedded proton pumps that acidify intracellular compartments in almost all eukaryotic cells. Homologous with ATP synthases, these multisubunit enzymes consist of a soluble catalytic V subcomplex and a membrane-embedded proton-translocating V subcomplex. The V and V subcomplexes can undergo reversible dissociation to regulate proton pumping, with reassociation of V and V requiring the protein complex known as RAVE (regulator of the ATPase of vacuoles and endosomes). In the yeast , RAVE consists of subunits Rav1p, Rav2p, and Skp1p. We used electron cryomicroscopy (cryo-EM) to determine a structure of yeast RAVE bound to V. In the structure, RAVE is an L-shaped complex with Rav2p pointing toward the membrane and Skp1p distant from both the membrane and V. Only Rav1p interacts with V, binding to a region of subunit A not found in the corresponding ATP synthase subunit. When bound to RAVE, V is in a rotational state suitable for binding the free V complex, but in the structure, it is partially disrupted, missing five of its 16 subunits. Other than these missing subunits and the conformation of the inhibitory subunit H, the V complex with RAVE appears poised for reassembly with V. PubMed: 39625975DOI: 10.1073/pnas.2414511121 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.7 Å) |
Structure validation
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