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dc.creatorFage, Christopher D.en
dc.creatorBrown, Dusty B.en
dc.creatorBoll, Joseph M.en
dc.creatorKeatinge-Clay, Adrian T.en
dc.creatorTrent, M. Stephenen
dc.date.accessioned2015-09-09T15:50:11Zen
dc.date.available2015-09-09T15:50:11Zen
dc.date.issued2014-10en
dc.identifier.citationFage, Christopher D., Brown, Dusty B., Boll, Joseph M., Keatinge-Clay, Adrian T., Trent, M. Stephen. >Crystallographic study of the phosphoethanolamine transferase EptC required for polymyxin resistance and motility in Campylobacter jejuni,> Acta Crystallogr D Biol Crystallogr. 2014 Oct;70(Pt 10):2730-9. doi: 10.1107/S1399004714017623. Epub 2014 Sep 27. doi: 10.1107/S1399004714017623en
dc.identifier.issn0907-4449en
dc.identifier.urihttp://hdl.handle.net/2152/31060en
dc.description.abstractThe foodborne enteric pathogen Campylobacter jejuni decorates a variety of its cell-surface structures with phosphoethanolamine (pEtN). Modifying lipid A with pEtN promotes cationic antimicrobial peptide resistance, whereas post-translationally modifying the flagellar rod protein FlgG with pEtN promotes flagellar assembly and motility, which are processes that are important for intestinal colonization. EptC, the pEtN transferase required for all known pEtN cell-surface modifications in C. jejuni, is a predicted inner-membrane metalloenzyme with a five-helix N-terminal transmembrane domain followed by a soluble sulfatase-like catalytic domain in the periplasm. The atomic structure of the catalytic domain of EptC (cEptC) was crystallized and solved to a resolution of 2.40 angstrom. cEptC adopts the alpha/beta/alpha fold of the sulfatase protein family and harbors a zinc-binding site. A phosphorylated Thr266 residue was observed that was hypothesized to mimic a covalent pEtN-enzyme intermediate. The requirement for Thr266 as well as the nearby residues Asn308, Ser309, His358 and His440 was ascertained via in vivo activity assays on mutant strains. The results establish a basis for the design of pEtN transferase inhibitors.en
dc.description.sponsorshipNational Institutes of Health (grants AI064184, AI076322, GM106112en
dc.description.sponsorshipArmy Research Office (grantW911NF-12-1-0390)en
dc.description.sponsorshipCollege of Natural Sciencesen
dc.description.sponsorshipOffice of the Executive Vice President and Provosten
dc.description.sponsorshipInstitute for Cellular and Molecular Biology at the University of Texas at Austinen
dc.description.sponsorshipUS DOE DE-AC02-06CH11357en
dc.description.sponsorshipNational Institute of General Medical Sciencesen
dc.description.sponsorshipHoward Hughes Medical Instituteen
dc.description.sponsorshipOffice of Science, Office of Basic Energy Sciences of the US Department of Energy DE-AC02-05CH11231en
dc.description.sponsorshipMaria Person and the Proteomics Facility at the University of Texas at Austin ES007784 (CRED) and RP110782 (CPRIT)en
dc.language.isoEnglishen
dc.rightsAdministrative deposit of works to Texas ScholarWorks: This works author(s) is or was a University faculty member, student or staff member; this article is already available through open access or the publisher allows a PDF version of the article to be freely posted online. The library makes the deposit as a matter of fair use (for scholarly, educational, and research purposes), and to preserve the work and further secure public access to the works of the University.en
dc.subjectguillain-barre-syndromeen
dc.subjectalkaline-phosphataseen
dc.subjectneisseria-meningitidisen
dc.subjectcrystal-structuresen
dc.subjectdata qualityen
dc.subjectinner-coreen
dc.subjectlipopolysaccharideen
dc.subjectmechanismen
dc.subjectlipooligosaccharideen
dc.subjectidentificationen
dc.subjectbiochemical research methodsen
dc.subjectbiochemistry & molecular biologyen
dc.subjectbiophysicsen
dc.subjectcrystallographyen
dc.titleCrystallographic Study Of The Phosphoethanolamine Transferase EptC required For Polymyxin Resistance And Motility In Campylobacter jejunien
dc.typeArticleen
dc.rights.holderen
dc.description.departmentMolecular Biosciencesen
dc.identifier.doi10.1107/s1399004714017623en
dc.identifier.urlen
dc.contributor.utaustinauthorFage, Christopher D.en
dc.contributor.utaustinauthorBrown, Dusty B.en
dc.contributor.utaustinauthorBoll, Joseph M.en
dc.contributor.utaustinauthorKeatinge-Clay, Adrian T.en
dc.contributor.utaustinauthorTrent, M. Stephenen
dc.relation.ispartofserialActa Crystallographica Section D-Biological Crystallographyen


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