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A new structural class of bacterial thioester domains reveals a slipknot topology
Author(s) -
Miller Ona K.,
Banfield Mark J.,
SchwarzLinek Ulrich
Publication year - 2018
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3478
Subject(s) - thioester , bacillus anthracis , enterococcus faecium , context (archaeology) , bacterial adhesin , bacteria , biology , microbiology and biotechnology , chemistry , computational biology , escherichia coli , biochemistry , genetics , gene , paleontology , enzyme
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.