{"oa_version":"None","type":"journal_article","citation":{"short":"L. Zhou, L.A. Sazanov, Science 365 (2019).","apa":"Zhou, L., &#38; Sazanov, L. A. (2019). Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase. <i>Science</i>. AAAS. <a href=\"https://doi.org/10.1126/science.aaw9144\">https://doi.org/10.1126/science.aaw9144</a>","ista":"Zhou L, Sazanov LA. 2019. Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase. Science. 365(6455), eaaw9144.","ama":"Zhou L, Sazanov LA. Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase. <i>Science</i>. 2019;365(6455). doi:<a href=\"https://doi.org/10.1126/science.aaw9144\">10.1126/science.aaw9144</a>","ieee":"L. Zhou and L. A. Sazanov, “Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase,” <i>Science</i>, vol. 365, no. 6455. AAAS, 2019.","mla":"Zhou, Long, and Leonid A. Sazanov. “Structure and Conformational Plasticity of the Intact Thermus Thermophilus V/A-Type ATPase.” <i>Science</i>, vol. 365, no. 6455, eaaw9144, AAAS, 2019, doi:<a href=\"https://doi.org/10.1126/science.aaw9144\">10.1126/science.aaw9144</a>.","chicago":"Zhou, Long, and Leonid A Sazanov. “Structure and Conformational Plasticity of the Intact Thermus Thermophilus V/A-Type ATPase.” <i>Science</i>. AAAS, 2019. <a href=\"https://doi.org/10.1126/science.aaw9144\">https://doi.org/10.1126/science.aaw9144</a>."},"publication_identifier":{"issn":["0036-8075"],"eissn":["1095-9203"]},"acknowledged_ssus":[{"_id":"ScienComp"}],"doi":"10.1126/science.aaw9144","_id":"6859","month":"08","issue":"6455","title":"Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase","publication_status":"published","scopus_import":"1","publisher":"AAAS","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","department":[{"_id":"LeSa"}],"language":[{"iso":"eng"}],"author":[{"orcid":"0000-0002-1864-8951","first_name":"Long","full_name":"Zhou, Long","last_name":"Zhou","id":"3E751364-F248-11E8-B48F-1D18A9856A87"},{"id":"338D39FE-F248-11E8-B48F-1D18A9856A87","last_name":"Sazanov","first_name":"Leonid A","orcid":"0000-0002-0977-7989","full_name":"Sazanov, Leonid A"}],"year":"2019","date_published":"2019-08-23T00:00:00Z","article_processing_charge":"No","article_number":"eaaw9144","publication":"Science","date_created":"2019-09-07T19:04:45Z","external_id":{"isi":["000482464000043"],"pmid":["31439765"]},"isi":1,"pmid":1,"volume":365,"related_material":{"link":[{"url":"https://ist.ac.at/en/news/structure-of-protein-nano-turbine-revealed/","relation":"press_release","description":"News on IST Website"}]},"day":"23","quality_controlled":"1","date_updated":"2023-08-29T07:52:02Z","intvolume":"       365","status":"public","abstract":[{"text":"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.","lang":"eng"}]}