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Science. 2019 Aug 23;365(6455). pii: eaaw9144. doi: 10.1126/science.aaw9144.

Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase.

Author information

1
Institute of Science and Technology Austria, Klosterneuberg 3400, Austria.
2
Institute of Science and Technology Austria, Klosterneuberg 3400, Austria. sazanov@ist.ac.at.

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 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 Thermus thermophilus V/A-ATPase, reconstituted into lipid nanodiscs, in three rotational states and two substates. These structures indicate substantial flexibility between V1 and Vo 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, V1-Vo torque transmission, and proton translocation, which are relevant for the entire V-type ATPase family.

PMID:
31439765
DOI:
10.1126/science.aaw9144

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