Premium
Clostridium difficile sortase recognizes a (S/P)PXTG sequence motif and can accommodate diaminopimelic acid as a substrate for transpeptidation
Author(s) -
van Leeuwen Hans C.,
Klychnikov Oleg I.,
Menks Mica A.C.,
Kuijper Ed J.,
Drijfhout Jan W.,
Hensbergen Paul J.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.09.041
Subject(s) - sortase , sortase a , diaminopimelic acid , biochemistry , biology , peptide sequence , microbiology and biotechnology , peptidoglycan , chemistry , gene , bacterial protein
Covalent attachment of surface proteins to the cell wall of Gram‐positive bacteria requires a sortase‐mediated transpeptidation reaction. In almost all Gram‐positive bacteria, the housekeeping sortase, sortase A, recognizes the canonical recognition sequence LPXTG (X = any amino acid). The human pathogen Clostridium difficile carries a single putative sortase gene ( cd2718 ) but neither transpeptidation activity nor specificity of CD2718 has been investigated. We produced recombinant CD2718 and examined its transpeptidation activity in vitro using synthetic peptides and MALDI‐ToF(‐ToF) MS analysis. We demonstrate that CD2718 has sortase activity with specificity for a (S/P)PXTG motif and can accommodate diaminopimelic acid as a substrate for transpeptidation.