A new structural class of bacterial thioester domains reveals a slipknot topology
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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.
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
Published by Wiley © 2018 The Authors. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
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.
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