Anchoring of surface proteins to the cell wall of Staphylococcus aureus: cysteine 184 and histidine 120 of sortase form a thiolate-imidazolium ion pair for catalysis
H Ton-That, SK Mazmanian, L Alksne… - Journal of Biological …, 2002 - ASBMB
Surface proteins of Staphylococcus aureus are anchored to the cell wall peptidoglycan by a
mechanism requiring a C-terminal sorting signal with a LPXTG motif. Sortase cleaves
polypeptides between the threonine and the glycine of the LPXTG motif. The carboxyl group
of threonine is subsequently amide-linked to the amino group of peptidoglycan cross-
bridges. The three-dimensional structure of sortase revealed the close proximity of the
catalytic site residue cysteine 184 with histidine 120; however, no structural evidence for a …
mechanism requiring a C-terminal sorting signal with a LPXTG motif. Sortase cleaves
polypeptides between the threonine and the glycine of the LPXTG motif. The carboxyl group
of threonine is subsequently amide-linked to the amino group of peptidoglycan cross-
bridges. The three-dimensional structure of sortase revealed the close proximity of the
catalytic site residue cysteine 184 with histidine 120; however, no structural evidence for a …
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