Crystal structure of scytalidoglutamic peptidase with its first potent inhibitor provides insights into substrate specificity and catalysis.

@article{Pillai2007CrystalSO,
  title={Crystal structure of scytalidoglutamic peptidase with its first potent inhibitor provides insights into substrate specificity and catalysis.},
  author={Bindu Pillai and Maia M. Cherney and Kazumi Hiraga and Katsumi Takada and Kohei Oda and Michael N. G. James},
  journal={Journal of molecular biology},
  year={2007},
  volume={365 2},
  pages={343-61}
}
Scytalidoglutamic peptidase (SGP) from Scytalidium lignicolum is the founding member of the newly discovered\ family of peptidases, G1, so far found exclusively in fungi. The crystal structure of SGP revealed a previously undescribed fold for peptidases and a unique catalytic dyad of residues Gln53 and Glu136. Surprisingly, the beta-sandwich structure of SGP is strikingly similar to members of the carbohydrate-binding concanavalin A-like lectins/glucanases superfamily. By analogy with the… CONTINUE READING

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