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A new structural class of bacterial thioester domains reveals a slipknot topology

DOI: 10.1002/pro.3478 DOI Help

Authors: Ona K. Miller (University of St Andrews) , Mark J. Banfield (John Innes Centre) , Ulrich Schwarz-linek (University of St Andrews)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Protein Science

State: Published (Approved)
Published: July 2018
Diamond Proposal Number(s): 10071 , 14980

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.

Journal Keywords: Bacterial surface proteins; TIE proteins; thioester domains; crystal structures; Bacillus anthracis; Staphylococcus aureus; Enterococcus faecium

Subject Areas: Biology and Bio-materials

Instruments: I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength)