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| Title | Oxidative stress protein Oxr1 promotes V-ATPase holoenzyme disassembly in catalytic activity-independent manner. |
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| Journal, issue, pages | EMBO J, Vol. 41, Issue 3, Page e109360, Year 2022 |
| Publish date | Feb 1, 2022 |
 Authors | Md Murad Khan / Seowon Lee / Sergio Couoh-Cardel / Rebecca A Oot / Hyunmin Kim / Stephan Wilkens / Soung-Hun Roh /   |
| PubMed Abstract | The vacuolar ATPase (V-ATPase) is a rotary motor proton pump that is regulated by an assembly equilibrium between active holoenzyme and autoinhibited V -ATPase and V proton channel subcomplexes. ...The vacuolar ATPase (V-ATPase) is a rotary motor proton pump that is regulated by an assembly equilibrium between active holoenzyme and autoinhibited V -ATPase and V proton channel subcomplexes. Here, we report cryo-EM structures of yeast V-ATPase assembled in vitro from lipid nanodisc reconstituted V and mutant V . Our analysis identified holoenzymes in three active rotary states, indicating that binding of V to V provides sufficient free energy to overcome V autoinhibition. Moreover, the structures suggest that the unequal spacing of V 's proton-carrying glutamic acid residues serves to alleviate the symmetry mismatch between V and V motors, a notion that is supported by mutagenesis experiments. We also uncover a structure of free V bound to Oxr1, a conserved but poorly characterized factor involved in the oxidative stress response. Biochemical experiments show that Oxr1 inhibits V -ATPase and causes disassembly of the holoenzyme, suggesting that Oxr1 plays a direct role in V-ATPase regulation. |
 External links | EMBO J / PubMed:34918374 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.8 - 6.6 Å |
| Structure data | EMDB-31538, PDB-7fda: EMDB-31539, PDB-7fdb: EMDB-31540, PDB-7fdc: EMDB-31541, PDB-7fde: |
| Source |
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 Keywords |  MOTOR PROTEIN / ATPase / proton pump / rotary motor enzyme / membrane protein |
