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dc.contributor.authorSimpson, Brent W.en_US
dc.contributor.authorOwens, Tristan W.en_US
dc.contributor.authorOrabella, Matthew J.en_US
dc.contributor.authorDavis, Rebecca M.en_US
dc.contributor.authorMay, Janine M.en_US
dc.contributor.authorTrauger, Sunia A.en_US
dc.contributor.authorKahne, Danielen_US
dc.contributor.authorRuiz, Natividaden_US
dc.date.accessioned2016-12-02T15:25:20Z
dc.date.issued2016en_US
dc.identifier.citationSimpson, Brent W., Tristan W. Owens, Matthew J. Orabella, Rebecca M. Davis, Janine M. May, Sunia A. Trauger, Daniel Kahne, and Natividad Ruiz. 2016. “Identification of Residues in the Lipopolysaccharide ABC Transporter That Coordinate ATPase Activity with Extractor Function.” mBio 7 (5): e01729-16. doi:10.1128/mBio.01729-16. http://dx.doi.org/10.1128/mBio.01729-16.en
dc.identifier.issn2150-7511en
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:29626140
dc.description.abstractABSTRACT The surface of most Gram-negative bacteria is covered with lipopolysaccharide (LPS), creating a permeability barrier against toxic molecules, including many antimicrobials. To assemble LPS on their surface, Gram-negative bacteria must extract newly synthesized LPS from the inner membrane, transport it across the aqueous periplasm, and translocate it across the outer membrane. The LptA to -G proteins assemble into a transenvelope complex that transports LPS from the inner membrane to the cell surface. The Lpt system powers LPS transport from the inner membrane by using a poorly characterized ATP-binding cassette system composed of the ATPase LptB and the transmembrane domains LptFG. Here, we characterize a cluster of residues in the groove region of LptB that is important for controlling LPS transport. We also provide the first functional characterization of LptFG and identify their coupling helices that interact with the LptB groove. Substitutions at conserved residues in these coupling helices compromise both the assembly and function of the LptB2FG complex. Defects in LPS transport conferred by alterations in the LptFG coupling helices can be rescued by changing a residue in LptB that is adjacent to functionally important residues in the groove region. This suppression is achieved by increasing the ATPase activity of the LptB2FG complex. Taken together, these data identify a specific binding site in LptB for the coupling helices of LptFG that is responsible for coupling of ATP hydrolysis by LptB with LptFG function to achieve LPS extraction.en
dc.language.isoen_USen
dc.publisherAmerican Society for Microbiologyen
dc.relation.isversionofdoi:10.1128/mBio.01729-16en
dc.relation.hasversionhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC5082905/pdf/en
dash.licenseLAAen_US
dc.titleIdentification of Residues in the Lipopolysaccharide ABC Transporter That Coordinate ATPase Activity with Extractor Functionen
dc.typeJournal Articleen_US
dc.description.versionVersion of Recorden
dc.relation.journalmBioen
dash.depositing.authorOwens, Tristan W.en_US
dc.date.available2016-12-02T15:25:20Z
dc.identifier.doi10.1128/mBio.01729-16*
dash.contributor.affiliatedOwens, Tristan
dash.contributor.affiliatedMay, Janine Margaret
dash.contributor.affiliatedKahne, Daniel
dash.contributor.affiliatedTrauger, Sunia


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