6fwy

Thioester domain of the Enterococcus faecium TIE86 protein

spinqualitylabelsall models 6fwy, resolution 2.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6fwy is a 4 chain structure with sequence from Enterococcus faecium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.14Å Ligands: GOL, PG4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1A7T0E1_ENTFC 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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