The 3D structure of thuricin CD, a two-component bacteriocin with cysteine sulfur to α-carbon cross-links.

@article{Sit2011The3S,
  title={The 3D structure of thuricin CD, a two-component bacteriocin with cysteine sulfur to α-carbon cross-links.},
  author={Clarissa S. Sit and R. Trent McKay and C. Ray Hill and R Paul Ross and John C Vederas},
  journal={Journal of the American Chemical Society},
  year={2011},
  volume={133 20},
  pages={7680-3}
}
Thuricin CD is an antimicrobial factor that consists of two peptides, Trn-α and Trn-β, that exhibit synergistic activity against drug resistant strains of Clostridium difficile. Trn-α and Trn-β each possess three sulfur to α-carbon thioether bridges for which the stereochemistry is unknown. This report presents the three-dimensional solution structures of Trn-α and Trn-β. Structure calculations were performed for the eight possible stereoisomers of each peptide based on the same NMR data. The… CONTINUE READING