An unusual orientation for Tyr75 in the active site of the aspartic proteinase from Saccharomyces cerevisiae.

@article{Gustchina2002AnUO,
  title={An unusual orientation for Tyr75 in the active site of the aspartic proteinase from Saccharomyces cerevisiae.},
  author={Alla Gustchina and Mi Li and Lowri H. Phylip and Wendy E. Lees and John Kay and Alexander Wlodawer},
  journal={Biochemical and biophysical research communications},
  year={2002},
  volume={295 4},
  pages={1020-6}
}
The structures of the native Saccharomyces cerevisiae proteinase A have been solved by molecular replacement in the monoclinic and trigonal crystal forms and refined at 2.6-2.7A resolution. These structures agree overall with those of other uninhibited aspartic proteinases. However, an unusual orientation for the side chain of Tyr75, a conserved residue on the flexible "flap" that covers the active site and is important for the activity of these enzymes, was found in the trigonal crystals. A… CONTINUE READING

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