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<titleInfo><title>Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase</title></titleInfo>


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<name type="personal">
  <namePart type="given">Long</namePart>
  <namePart type="family">Zhou</namePart>
  <role><roleTerm type="text">author</roleTerm> </role><identifier type="local">3E751364-F248-11E8-B48F-1D18A9856A87</identifier><description xsi:type="identifierDefinition" type="orcid">0000-0002-1864-8951</description></name>
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  <namePart type="given">Leonid A</namePart>
  <namePart type="family">Sazanov</namePart>
  <role><roleTerm type="text">author</roleTerm> </role><identifier type="local">338D39FE-F248-11E8-B48F-1D18A9856A87</identifier><description xsi:type="identifierDefinition" type="orcid">0000-0002-0977-7989</description></name>







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<abstract lang="eng">V (vacuolar)/A (archaeal)-type adenosine triphosphatases (ATPases), found in archaeaand eubacteria, couple ATP hydrolysis or synthesis to proton translocation across theplasma membrane using the rotary-catalysis mechanism. They belong to the V-typeATPase family, which differs from the mitochondrial/chloroplast F-type ATP synthasesin overall architecture. We solved cryo–electron microscopy structures of the intactThermus thermophilusV/A-ATPase, reconstituted into lipid nanodiscs, in three rotationalstates and two substates. These structures indicate substantial flexibility betweenV1and Voin a working enzyme, which results from mechanical competition between centralshaft rotation and resistance from the peripheral stalks. We also describedetails of adenosine diphosphate inhibition release, V1-Votorque transmission, andproton translocation, which are relevant for the entire V-type ATPase family.</abstract>

<originInfo><publisher>AAAS</publisher><dateIssued encoding="w3cdtf">2019</dateIssued>
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<relatedItem type="host"><titleInfo><title>Science</title></titleInfo>
  <identifier type="issn">0036-8075</identifier>
  <identifier type="eIssn">1095-9203</identifier>
  <identifier type="MEDLINE">31439765</identifier>
  <identifier type="ISI">000482464000043</identifier><identifier type="doi">10.1126/science.aaw9144</identifier>
<part><detail type="volume"><number>365</number></detail><detail type="issue"><number>6455</number></detail>
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     <url>https://ist.ac.at/en/news/structure-of-protein-nano-turbine-revealed/</url>
  
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<ista>Zhou L, Sazanov LA. 2019. Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase. Science. 365(6455), eaaw9144.</ista>
<mla>Zhou, Long, and Leonid A. Sazanov. “Structure and Conformational Plasticity of the Intact Thermus Thermophilus V/A-Type ATPase.” &lt;i&gt;Science&lt;/i&gt;, vol. 365, no. 6455, eaaw9144, AAAS, 2019, doi:&lt;a href=&quot;https://doi.org/10.1126/science.aaw9144&quot;&gt;10.1126/science.aaw9144&lt;/a&gt;.</mla>
<short>L. Zhou, L.A. Sazanov, Science 365 (2019).</short>
<chicago>Zhou, Long, and Leonid A Sazanov. “Structure and Conformational Plasticity of the Intact Thermus Thermophilus V/A-Type ATPase.” &lt;i&gt;Science&lt;/i&gt;. AAAS, 2019. &lt;a href=&quot;https://doi.org/10.1126/science.aaw9144&quot;&gt;https://doi.org/10.1126/science.aaw9144&lt;/a&gt;.</chicago>
<apa>Zhou, L., &amp;#38; Sazanov, L. A. (2019). Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase. &lt;i&gt;Science&lt;/i&gt;. AAAS. &lt;a href=&quot;https://doi.org/10.1126/science.aaw9144&quot;&gt;https://doi.org/10.1126/science.aaw9144&lt;/a&gt;</apa>
<ama>Zhou L, Sazanov LA. Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase. &lt;i&gt;Science&lt;/i&gt;. 2019;365(6455). doi:&lt;a href=&quot;https://doi.org/10.1126/science.aaw9144&quot;&gt;10.1126/science.aaw9144&lt;/a&gt;</ama>
<ieee>L. Zhou and L. A. Sazanov, “Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase,” &lt;i&gt;Science&lt;/i&gt;, vol. 365, no. 6455. AAAS, 2019.</ieee>
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