6FWY

Thioester domain of the Enterococcus faecium TIE86 protein

Summary for 6FWY

• Entry DOI: 10.2210/pdb6fwy/pdb
• Related: 6FWV 6FX6
• Descriptor: B-type Cna protein, TETRAETHYLENE GLYCOL, GLYCEROL, ... (4 entities in total)
• Functional Keywords: lpxtg-anchored, surface protein, thioester domain, tie protein, unknown function
• Biological source: Enterococcus faecium (Streptococcus faecium)
• Total number of polymer chains: 4
• Total formula weight: 121757.98

Authors

Miller, O.K.,Banfield, M.J.,Schwarz-Linek, U. (deposition date: 2018-03-07, release date: 2018-08-08, Last modification date: 2024-05-08)

Primary citation

Miller, O.K.,Banfield, M.J.,Schwarz-Linek, U.
A new structural class of bacterial thioester domains reveals a slipknot topology.
Protein Sci., 27:1651-1660, 2018

PubMed 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.

PubMed: 30052296
DOI: 10.1002/pro.3478

Experimental method

X-RAY DIFFRACTION (2.14 Å)