Mutagenesis studies of substrate recognition and catalysis in the sortase A transpeptidase from Staphylococcus aureus.

@article{Bentley2008MutagenesisSO,
  title={Mutagenesis studies of substrate recognition and catalysis in the sortase A transpeptidase from Staphylococcus aureus.},
  author={Matthew L. Bentley and Erin C Lamb and Dewey G. McCafferty},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 21},
  pages={14762-71}
}
The Staphylococcus aureus transpeptidase sortase A (SrtA) is responsible for anchoring a range of virulence- and colonization-associated proteins to the cell wall. SrtA recognizes substrates that contain a C-terminal LPXTG motif. This sequence is cleaved following the threonine, and an amide bond is formed between the threonine and the pentaglycine cross-bridge of branched lipid II. Previous studies have implicated the beta6/beta7 loop region of SrtA in LPXTG recognition but have not… CONTINUE READING