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| Title | A distinct inhibitory mechanism of the V-ATPase by Vibrio VopQ revealed by cryo-EM. |
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| Journal, issue, pages | Nat Struct Mol Biol, Vol. 27, Issue 6, Page 589-597, Year 2020 |
| Publish date | May 18, 2020 |
 Authors | Wei Peng / Amanda K Casey / Jessie Fernandez / Emily M Carpinone / Kelly A Servage / Zhe Chen / Yang Li / Diana R Tomchick / Vincent J Starai / Kim Orth /  |
| PubMed Abstract | The Vibrio parahaemolyticus T3SS effector VopQ targets host-cell V-ATPase, resulting in blockage of autophagic flux and neutralization of acidic compartments. Here, we report the cryo-EM structure of ...The Vibrio parahaemolyticus T3SS effector VopQ targets host-cell V-ATPase, resulting in blockage of autophagic flux and neutralization of acidic compartments. Here, we report the cryo-EM structure of VopQ bound to the V subcomplex of the V-ATPase. VopQ inserts into membranes and forms an unconventional pore while binding directly to subunit c of the V-ATPase membrane-embedded subcomplex V. We show that VopQ arrests yeast growth in vivo by targeting the immature V subcomplex in the endoplasmic reticulum (ER), thus providing insight into the observation that VopQ kills cells in the absence of a functional V-ATPase. VopQ is a bacterial effector that has been discovered to inhibit a host-membrane megadalton complex by coincidentally binding its target, inserting into a membrane and disrupting membrane potential. Collectively, our results reveal a mechanism by which bacterial effectors modulate host cell biology and provide an invaluable tool for future studies on V-ATPase-mediated membrane fusion and autophagy. |
 External links | Nat Struct Mol Biol / PubMed:32424347 |
| Methods | EM (single particle) |
| Resolution | 3.1 - 3.2 Å |
| Structure data | EMDB-20322, PDB-6pe4: EMDB-20323, PDB-6pe5: |
| Source |
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 Keywords |  TRANSPORT PROTEIN / complex |
