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A new structural class of bacterial thioester domains reveals a slipknot topology
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dc.contributor.author | Miller, Ona Kealoha | |
dc.contributor.author | Banfield, Mark | |
dc.contributor.author | Schwarz-Linek, Ulrich | |
dc.date.accessioned | 2018-09-27T15:30:09Z | |
dc.date.available | 2018-09-27T15:30:09Z | |
dc.date.issued | 2018-09 | |
dc.identifier | 255169503 | |
dc.identifier | 4ba2420d-ec41-45f0-8a0b-415506768d4d | |
dc.identifier | 85053814784 | |
dc.identifier | 000447779000010 | |
dc.identifier.citation | Miller , 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 . https://doi.org/10.1002/pro.3478 | en |
dc.identifier.issn | 1469-896X | |
dc.identifier.other | ORCID: /0000-0003-0526-223X/work/48774872 | |
dc.identifier.uri | https://hdl.handle.net/10023/16091 | |
dc.description | This 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.abstract | An 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.format.extent | 1452782 | |
dc.language.iso | eng | |
dc.relation.ispartof | Protein Science | en |
dc.subject | Bacterial surface proteins | en |
dc.subject | TIE proteins | en |
dc.subject | Thioester domains | en |
dc.subject | Crystal structures | en |
dc.subject | Bacillus anthracis | en |
dc.subject | Staphylococcus aureus | en |
dc.subject | Enterococcus faecium | en |
dc.subject | QD Chemistry | en |
dc.subject | QH301 Biology | en |
dc.subject | Structural Biology | en |
dc.subject | Immunology and Microbiology (miscellaneous) | en |
dc.subject | DAS | en |
dc.subject.lcc | QD | en |
dc.subject.lcc | QH301 | en |
dc.title | A new structural class of bacterial thioester domains reveals a slipknot topology | en |
dc.type | Journal article | en |
dc.contributor.sponsor | Medical Research Council | en |
dc.contributor.institution | University of St Andrews. School of Biology | en |
dc.contributor.institution | University of St Andrews. Biomedical Sciences Research Complex | en |
dc.identifier.doi | 10.1002/pro.3478 | |
dc.description.status | Peer reviewed | en |
dc.identifier.grantnumber | MR/K001485/1 | en |
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