The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands.

@article{Tame1995TheCS,
  title={The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands.},
  author={Jeremy R.H. Tame and Eleanor J. Dodson and Garib N Murshudov and Christopher F. Higgins and Anthony James Wilkinson},
  journal={Structure},
  year={1995},
  volume={3 12},
  pages={1395-406}
}
BACKGROUND The periplasmic oligopeptide-binding protein OppA has a remarkably broad substrate specificity, binding peptides of two or five amino-acid residues with high affinity, but little regard to sequence. It is therefore an ideal system for studying how different chemical groups can be accommodated in a protein interior. The ability of the protein to bind peptides of different lengths has been studied by co-crystallising it with different ligands. RESULTS Crystals of OppA from Salmonella… CONTINUE READING

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