Mechanism of stabilization of a bacterial collagen triple helix in the absence of hydroxyproline.

@article{Mohs2007MechanismOS,
  title={Mechanism of stabilization of a bacterial collagen triple helix in the absence of hydroxyproline.},
  author={Angela Mohs and Teresita Silva and Takeshi Yoshida and Ravish Amin and Slawomir Lukomski and M. Inouye and Barbara Brodsky},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 41},
  pages={29757-65}
}
The Streptococcus pyogenes cell-surface protein Scl2 contains a globular N-terminal domain and a collagen-like domain, (Gly-Xaa-X'aa)(79), which forms a triple helix with a thermal stability close to that seen for mammalian collagens. Hyp is a major contributor to triple-helix stability in animal collagens, but is not present in bacteria, which lack prolyl hydroxylase. To explore the basis of bacterial collagen triple-helix stability in the absence of Hyp, biophysical studies were carried out… CONTINUE READING

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