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EC Number
General Information
Commentary
Reference
evolution
the enzyme is a member of the sortase cysteine transpeptidase family. Members of this enzyme superfamily are widely distributed in Gram-positive bacteria that frequently utilize multiple sortases to elaborate their peptidoglycan, and the family members have a conserved active site His-Cys-Arg triad that joins a sorting signal located at the C-terminus of their protein substrate to an amino nucleophile located on the cell surface
more
analysis of the substrate binding structure of the enzyme using SrtB-NPQT complexes, by computational modeling, molecular dynamics simulations, and targeted amino acid mutagenesis revealing that the backbone amide of Glu224 and the side chain of Arg233 form an oxyanion hole in sortase B that stabilizes high energy tetrahedral catalytic intermediates. A highly conserved threonine residue within the bound sorting signal substrate facilitates construction of the oxyanion hole by stabilizing the position of the active site arginine residue via hydrogen bonding
physiological function
sortase attaches hemoproteins to the cell wall
physiological function
sortase cysteine transpeptidases covalently attach proteins to the bacterial cell wall or assemble fiber-like pili that promote bacterial adhesion
physiological function
the class B sortase is involved in pilus assembly
Results 1 - 5 of 5