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| Title | Structure and conformational plasticity of the intact V/A-type ATPase. |
|---|---|
| Journal, issue, pages | Science, Vol. 365, Issue 6455, Year 2019 |
| Publish date | Aug 23, 2019 |
 Authors | Long Zhou / Leonid A Sazanov /  |
| PubMed Abstract | V (vacuolar)/A (archaeal)-type adenosine triphosphatases (ATPases), found in archaea and eubacteria, couple ATP hydrolysis or synthesis to proton translocation across the plasma membrane using the ...V (vacuolar)/A (archaeal)-type adenosine triphosphatases (ATPases), found in archaea and eubacteria, couple ATP hydrolysis or synthesis to proton translocation across the plasma membrane using the rotary-catalysis mechanism. They belong to the V-type ATPase family, which differs from the mitochondrial/chloroplast F-type ATP synthases in overall architecture. We solved cryo-electron microscopy structures of the intact V/A-ATPase, reconstituted into lipid nanodiscs, in three rotational states and two substates. These structures indicate substantial flexibility between V and V in a working enzyme, which results from mechanical competition between central shaft rotation and resistance from the peripheral stalks. We also describe details of adenosine diphosphate inhibition release, V-V torque transmission, and proton translocation, which are relevant for the entire V-type ATPase family. |
 External links | Science / PubMed:31439765 |
| Methods | EM (single particle) |
| Resolution | 3.25 - 4.3 Å |
| Structure data | EMDB-4640, PDB-6qum: EMDB-4699, PDB-6r0w: EMDB-4700, PDB-6r0y: |
| Chemicals |  ChemComp-MG:  ChemComp-ADP: |
| Source |
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 Keywords |  MEMBRANE PROTEIN / ATP hydrolysis/synthesis / proton translocation / rotary catalysis |
