Zhou 2019 Science: Difference between revisions
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{{Publication | {{Publication | ||
|title=Zhou L, Sazanov LA (2019) Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase. Science 365:eaaw9144. doi | |title=Zhou L, Sazanov LA (2019) Structure and conformational plasticity of the intact ''Thermus thermophilus'' V/A-type ATPase. Science 365:eaaw9144. https://doi.org/10.1126/science.aaw9144 | ||
|info=[https://pubmed.ncbi.nlm.nih.gov/31439765/ PMID: 31439765] | |info=[https://pubmed.ncbi.nlm.nih.gov/31439765/ PMID: 31439765] | ||
|authors=Zhou L, Sazanov Leonid A | |authors=Zhou L, Sazanov Leonid A |
Latest revision as of 20:06, 6 November 2023
Zhou L, Sazanov LA (2019) Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase. Science 365:eaaw9144. https://doi.org/10.1126/science.aaw9144 |
Zhou L, Sazanov Leonid A (2019) Science
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.
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Enzyme: Complex V;ATP synthase Regulation: Coupling efficiency;uncoupling