6C6L
Yeast Vacuolar ATPase Vo in lipid nanodisc
Summary for 6C6L
| Entry DOI | 10.2210/pdb6c6l/pdb |
| EMDB information | 7348 |
| Descriptor | V-type proton ATPase subunit c', V-type proton ATPase subunit c'', V0 assembly protein 1, ... (8 entities in total) |
| Functional Keywords | vacuolar h+-atpase, vo proton channel, rotary motor enzyme, membrane protein |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 15 |
| Total formula weight | 353416.86 |
| Authors | Roh, S.,Stam, N.J.,Hryc, C.,Couoh-Cardel, S.,Pintilie, G.,Chiu, W.,Wilkens, S. (deposition date: 2018-01-19, release date: 2018-03-21, Last modification date: 2024-03-13) |
| Primary citation | Roh, S.H.,Stam, N.J.,Hryc, C.F.,Couoh-Cardel, S.,Pintilie, G.,Chiu, W.,Wilkens, S. The 3.5- angstrom CryoEM Structure of Nanodisc-Reconstituted Yeast Vacuolar ATPase VoProton Channel. Mol. Cell, 69:993-1004.e3, 2018 Cited by PubMed Abstract: The molecular mechanism of transmembrane proton translocation in rotary motor ATPases is not fully understood. Here, we report the 3.5-Å resolution cryoEM structure of the lipid nanodisc-reconstituted V proton channel of the yeast vacuolar H-ATPase, captured in a physiologically relevant, autoinhibited state. The resulting atomic model provides structural detail for the amino acids that constitute the proton pathway at the interface of the proteolipid ring and subunit a. Based on the structure and previous mutagenesis studies, we propose the chemical basis of transmembrane proton transport. Moreover, we discovered that the C terminus of the assembly factor Voa1 is an integral component of mature V. Voa1's C-terminal transmembrane α helix is bound inside the proteolipid ring, where it contributes to the stability of the complex. Our structure rationalizes possible mechanisms by which mutations in human V can result in disease phenotypes and may thus provide new avenues for therapeutic interventions. PubMed: 29526695DOI: 10.1016/j.molcel.2018.02.006 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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