6fx6

Publication Abstract from PubMed

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 beta-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. This article is protected by copyright. All rights reserved.

A new structural class of bacterial thioester domains reveals a slipknot topology.,Miller OK, Banfield MJ, Schwarz-Linek U Protein Sci. 2018 Jul 27. doi: 10.1002/pro.3478. PMID:30052296^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.