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dc.contributor.authorMiller, Ona Kealoha
dc.contributor.authorBanfield, Mark
dc.contributor.authorSchwarz-Linek, Ulrich
dc.identifier.citationMiller , O K , Banfield , M & Schwarz-Linek , U 2018 , ' A new structural class of bacterial thioester domains reveals a slipknot topology ' , Protein Science , vol. 27 , no. 9 , pp. 1651-1660 .
dc.identifier.otherORCID: /0000-0003-0526-223X/work/48774872
dc.descriptionThis work was supported by the MRC, UK grant MR/K001485 for MJB, USL; the BBSRC, UK grant BB/J00453 and the John Innes Foundation for MJB; The Royal Society of Edinburgh and the Carnegie Trust for OKM.en
dc.description.abstractAn increasing number of surface‐associated proteins identified in Gram‐positive bacteria are characterized by intramolecular cross‐links in structurally conserved thioester, isopeptide, and ester domains (TIE proteins). Two classes of thioester domains (TEDs) have been predicted based on sequence with, to date, only representatives of Class I structurally characterized. Here, we present crystal structures of three Class II TEDs from Bacillus anthracis, vancomycin‐resistant Staphylococcus aureus, and vancomycin‐resistant Enterococcus faecium. These proteins are structurally distinct from Class I TEDs due to a β‐sandwich domain that is inserted into the conserved TED fold to form a slipknot structure. Further, the B. anthracis TED domain is presented in the context of a full‐length sortase‐anchored protein structure (BaTIE). This provides insight into the three‐dimensional arrangement of TIE proteins, which emerge as very abundant putative adhesins of Gram‐positive bacteria.
dc.relation.ispartofProtein Scienceen
dc.subjectBacterial surface proteinsen
dc.subjectTIE proteinsen
dc.subjectThioester domainsen
dc.subjectCrystal structuresen
dc.subjectBacillus anthracisen
dc.subjectStaphylococcus aureusen
dc.subjectEnterococcus faeciumen
dc.subjectQD Chemistryen
dc.subjectQH301 Biologyen
dc.subjectStructural Biologyen
dc.subjectImmunology and Microbiology (miscellaneous)en
dc.titleA new structural class of bacterial thioester domains reveals a slipknot topologyen
dc.typeJournal articleen
dc.contributor.sponsorMedical Research Councilen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.description.statusPeer revieweden

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