A slow-forming isopeptide bond in the structure of the major pilin SpaD from Corynebacterium diphtheriae has implications for pilus assembly

@inproceedings{Kang2014ASI,
  title={A slow-forming isopeptide bond in the structure of the major pilin SpaD from Corynebacterium diphtheriae has implications for pilus assembly},
  author={Hae Joo Kang and Neil G Paterson and Chae Un Kim and Martin James Middleditch and Chungyu Chang and Hung Ton-That and Edward N Baker},
  booktitle={Acta crystallographica. Section D, Biological crystallography},
  year={2014}
}
The Gram-positive organism Corynebacterium diphtheriae, the cause of diphtheria in humans, expresses pili on its surface which it uses for adhesion and colonization of its host. These pili are covalent protein polymers composed of three types of pilin subunit that are assembled by specific sortase enzymes. A structural analysis of the major pilin SpaD, which forms the polymeric backbone of one of the three types of pilus expressed by C. diphtheriae, is reported. Mass-spectral and… CONTINUE READING
Highly Cited
This paper has 25 citations. REVIEW CITATIONS
Recent Discussions
This paper has been referenced on Twitter 2 times over the past 90 days. VIEW TWEETS

References

Publications referenced by this paper.
Showing 1-3 of 3 references

Acta Cryst

  • W. Kabsch
  • D66, 125–132.
  • 2010
Highly Influential
4 Excerpts

PLoS One, 5, e10919

  • I.
  • Studier, F. W. (2005). Protein Expr. Purif. 41…
  • 2010
Highly Influential
2 Excerpts

J

  • L.S.V.
  • Mol. Biol. 407, 731–743. Vetsch, M., Puorger, C…
  • 2011

Similar Papers

Loading similar papers…