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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 <jats:italic>Bacillus anthracis<\/jats:italic>, vancomycin\u2010resistant <jats:italic>Staphylococcus aureus<\/jats:italic>, and vancomycin\u2010resistant <jats:italic>Enterococcus faecium.<\/jats:italic> These proteins are structurally distinct from Class I TEDs due to a \u03b2\u2010sandwich domain that is inserted into the conserved TED fold to form a slipknot structure. Further, the <jats:italic>B. anthracis<\/jats:italic> TED domain is presented in the context of a full\u2010length sortase\u2010anchored protein structure (BaTIE). This provides insight into the three\u2010dimensional arrangement of TIE proteins, which emerge as very abundant putative adhesins of Gram\u2010positive bacteria.<\/jats:p>","DOI":"10.1002\/pro.3478","type":"journal-article","created":{"date-parts":[[2018,7,27]],"date-time":"2018-07-27T15:08:47Z","timestamp":1532704127000},"page":"1651-1660","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["A new structural class of bacterial thioester domains reveals a slipknot topology"],"prefix":"10.1002","volume":"27","author":[{"given":"Ona K.","family":"Miller","sequence":"first","affiliation":[{"name":"Biomedical Sciences Research Complex and School of Biology University of St Andrews  St Andrews KY16 9ST United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark J.","family":"Banfield","sequence":"additional","affiliation":[{"name":"John Innes Centre, Department of Biological Chemistry Norwich 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