{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,2]],"date-time":"2026-09-02T10:17:31Z","timestamp":1788344251192,"version":"build-2803163510"},"reference-count":48,"publisher":"American Society for Microbiology","issue":"4","license":[{"start":{"date-parts":[[2019,7,2]],"date-time":"2019-07-02T00:00:00Z","timestamp":1562025600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/doi.org\/10.1128\/AuthorWarrantyLicense.v1"},{"start":{"date-parts":[[2019,8,27]],"date-time":"2019-08-27T00:00:00Z","timestamp":1566864000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/100000002","name":"HHS | National Institutes of Health","doi-asserted-by":"publisher","award":["R01AI145069"],"award-info":[{"award-number":["R01AI145069"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["mBio"],"published-print":{"date-parts":[[2019,8,27]]},"abstract":"<jats:p>\n                    <jats:named-content content-type=\"genus-species\">Acinetobacter baumannii<\/jats:named-content>\n                    is a successful human pathogen which has emerged as one of the most problematic and highly antibiotic-resistant Gram-negative bacteria worldwide. Multidrug efflux is a major mechanism that\n                    <jats:named-content content-type=\"genus-species\">A. baumannii<\/jats:named-content>\n                    uses to counteract the action of multiple classes of antibiotics, such as \u03b2-lactams, tetracyclines, fluoroquinolones, and aminoglycosides. Here, we report a cryo-electron microscopy (cryo-EM) structure of the prevalent\n                    <jats:named-content content-type=\"genus-species\">A. baumannii<\/jats:named-content>\n                    AdeB multidrug efflux pump, which indicates a plausible pathway for multidrug extrusion. Overall, our data suggest a mechanism for energy coupling that powers up this membrane protein to export antibiotics from bacterial cells. Our studies will ultimately inform an era in structure-guided drug design to combat multidrug resistance in these Gram-negative pathogens.\n                  <\/jats:p>","DOI":"10.1128\/mbio.01295-19","type":"journal-article","created":{"date-parts":[[2019,7,1]],"date-time":"2019-07-01T06:41:46Z","timestamp":1561963306000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":77,"title":["Cryo-Electron Microscopy Structure of an Acinetobacter baumannii Multidrug Efflux Pump"],"prefix":"10.1128","volume":"10","author":[{"given":"Chih-Chia","family":"Su","sequence":"first","affiliation":[{"name":"Department of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher E.","family":"Morgan","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, Case Western Reserve University School of Medicine, 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