6M0R
2.7A Yeast Vo state3
Summary for 6M0R
| Entry DOI | 10.2210/pdb6m0r/pdb |
| EMDB information | 30034 |
| Descriptor | V-type proton ATPase subunit c', 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine, PYROPHOSPHATE, ... (13 entities in total) |
| Functional Keywords | v-atpase, vo sub-complex, cryoem, transport protein |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 15 |
| Total formula weight | 346827.82 |
| Authors | Roh, S.H.,Shekhar, M.,Pintilie, G.,Chipot, C.,Wilkens, S.,Singharoy, A.,Chiu, W. (deposition date: 2020-02-22, release date: 2020-11-04, Last modification date: 2024-03-27) |
| Primary citation | Roh, S.H.,Shekhar, M.,Pintilie, G.,Chipot, C.,Wilkens, S.,Singharoy, A.,Chiu, W. Cryo-EM and MD infer water-mediated proton transport and autoinhibition mechanisms of V o complex. Sci Adv, 6:-, 2020 Cited by PubMed Abstract: Rotary vacuolar adenosine triphosphatases (V-ATPases) drive transmembrane proton transport through a V proton channel subcomplex. Despite recent high-resolution structures of several rotary ATPases, the dynamic mechanism of proton pumping remains elusive. Here, we determined a 2.7-Å cryo-electron microscopy (cryo-EM) structure of yeast V proton channel in nanodisc that reveals the location of ordered water molecules along the proton path, details of specific protein-lipid interactions, and the architecture of the membrane scaffold protein. Moreover, we uncover a state of V that shows the -ring rotated by ~14°. Molecular dynamics simulations demonstrate that the two rotary states are in thermal equilibrium and depict how the protonation state of essential glutamic acid residues couples water-mediated proton transfer with -ring rotation. Our cryo-EM models and simulations also rationalize a mechanism for inhibition of passive proton transport as observed for free V that is generated as a result of V-ATPase regulation by reversible disassembly in vivo. PubMed: 33028525DOI: 10.1126/sciadv.abb9605 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.7 Å) |
Structure validation
Download full validation report
