The full-length Streptococcus pneumoniae major pilin RrgB crystallizes in a fibre-like structure, which presents the D1 isopeptide bond and provides details on the mechanism of pilus polymerization.

@article{Mortaji2012TheFS,
  title={The full-length Streptococcus pneumoniae major pilin RrgB crystallizes in a fibre-like structure, which presents the D1 isopeptide bond and provides details on the mechanism of pilus polymerization.},
  author={Lamya El Mortaji and Carlos Contreras-Martel and Monica Moschioni and Ilaria Ferlenghi and Clothilde Manzano and Thierry Vernet and Andr{\'e}a Dessen and Anne Marie Di Guilmi},
  journal={The Biochemical journal},
  year={2012},
  volume={441 3},
  pages={833-41}
}
RrgB is the major pilin which forms the pneumococcal pilus backbone. We report the high-resolution crystal structure of the full-length form of RrgB containing the IPQTG sorting motif. The RrgB fold is organized into four distinct domains, D1-D4, each of which is stabilized by an isopeptide bond. Crystal packing revealed a head-to-tail organization involving the interaction of the IPQTG motif into the D1 domain of two successive RrgB monomers. This fibrillar assembly, which fits into the… CONTINUE READING
14 Citations
43 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 14 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 43 references

Similar Papers

Loading similar papers…