Structural and biochemical analyses of a Clostridium perfringens sortase D transpeptidase

@inproceedings{Suryadinata2015StructuralAB,
  title={Structural and biochemical analyses of a Clostridium perfringens sortase D transpeptidase},
  author={Randy Suryadinata and Shane A. Seabrook and Timothy E. Adams and Stewart D. Nuttall and Thomas S. Peat},
  booktitle={Acta crystallographica. Section D, Biological crystallography},
  year={2015}
}
The assembly and anchorage of various pathogenic proteins on the surface of Gram-positive bacteria is mediated by the sortase family of enzymes. These cysteine transpeptidases catalyze a unique sorting signal motif located at the C-terminus of their target substrate and promote the covalent attachment of these proteins onto an amino nucleophile located on another protein or on the bacterial cell wall. Each of the six distinct classes of sortases displays a unique biological role, with… CONTINUE READING
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References

Publications referenced by this paper.
Showing 1-4 of 4 references

Pathogens and Toxins in Foods: Challenges and Interventions

V. K. Jenuja, J. S. Novak, R. J. Labbe
2010
View 5 Excerpts
Highly Influenced

Acta Cryst

K. Persson
D67, 212–217. • 2011

J

N. Stein
Appl. Cryst. 41, 641–643. • 2008
View 2 Excerpts

Food Microbiology: Fundamentals and Frontiers, edited by M

B. A. McClane
P. Doyle & L. R. Beuchat, pp. 423–444. Washington: ASM Press. • 2007
View 2 Excerpts

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