Journal
PROTEIN SCIENCE
Volume 27, Issue 9, Pages 1651-1660Publisher
WILEY
DOI: 10.1002/pro.3478
Keywords
bacterial surface proteins; TIE proteins; thioester domains; crystal structures; Bacillus anthracis; Staphylococcus aureus; Enterococcus faecium
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Funding
- Biotechnology and Biological Sciences Research Council [BB/J00453]
- Medical Research Council [MR/K001485]
- Diamond Light Source [MX14980, MX10071]
- Royal Society of Edinburgh
- John Innes Foundation
- BBSRC [BBS/E/J/000CA506, BBS/E/J/000PR9795] Funding Source: UKRI
- MRC [MR/K001485/1] Funding Source: UKRI
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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 -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.
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