{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T03:00:17Z","timestamp":1791428417507,"version":"4.3.3"},"reference-count":55,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2020,4,14]],"date-time":"2020-04-14T00:00:00Z","timestamp":1586822400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["GM100951"],"award-info":[{"award-number":["GM100951"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2020,8]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Lipopolysaccharides (LPS) are essential envelope components in many Gram\u2010negative bacteria and provide intrinsic resistance to antibiotics. LPS molecules are synthesized in the inner membrane and then transported to the cell surface by the LPS transport (Lpt) machinery. In this system, the ATP\u2010binding cassette (ABC) transporter LptB\n                    <jats:sub>2<\/jats:sub>\n                    FGC extracts LPS from the inner membrane and places it onto a periplasmic protein bridge through a poorly understood mechanism. Here, we show that residue E86 of LptB is essential for coupling the function of this ATPase to that of its partners LptFG, specifically at the step where ATP binding drives the closure of the LptB dimer and the collapse of the LPS\u2010binding cavity in LptFG that moves LPS to the Lpt periplasmic bridge. We also show that defects caused by changing residue E86 are suppressed by mutations altering either LPS structure or transmembrane helices in LptG. Furthermore, these suppressors also fix defects in the coupling helix of LptF, but not of LptG. Together, these results support a transport mechanism in which the ATP\u2010driven movements of LptB and those of the substrate\u2010binding cavity in LptFG are bi\u2010directionally coordinated through the rigid\u2010body coupling, with LptF\u2019s coupling helix being important in coordinating cavity collapse with LptB dimerization.\n                  <\/jats:p>","DOI":"10.1111\/mmi.14506","type":"journal-article","created":{"date-parts":[[2020,3,31]],"date-time":"2020-03-31T21:21:57Z","timestamp":1585689717000},"page":"200-213","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":21,"title":["LptB\u2010LptF coupling mediates the closure of the substrate\u2010binding cavity in the LptB\n                    <sub>2<\/sub>\n                    FGC transporter through a rigid\u2010body mechanism to extract LPS"],"prefix":"10.1111","volume":"114","author":[{"given":"Emily A.","family":"Lundstedt","sequence":"first","affiliation":[{"name":"Department of Microbiology The Ohio State University Columbus OH USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brent W.","family":"Simpson","sequence":"additional","affiliation":[{"name":"Department of Microbiology The Ohio State University Columbus OH USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6369-2206","authenticated-orcid":false,"given":"Natividad","family":"Ruiz","sequence":"additional","affiliation":[{"name":"Department of Microbiology The Ohio State University Columbus OH 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