Direct observation by X-ray analysis of the tetrahedral "intermediate" of aspartic proteinases.

@article{Veerapandian1992DirectOB,
  title={Direct observation by X-ray analysis of the tetrahedral "intermediate" of aspartic proteinases.},
  author={B Veerapandian and Jon B. Cooper and Andrej Sali and Tom L. Blundell and Robert L Rosati and Beryl W. Dominy and D B Damon and Dennis J. Hoover},
  journal={Protein science : a publication of the Protein Society},
  year={1992},
  volume={1 3},
  pages={322-8}
}
We report the X-ray analysis at 2.0 A resolution for crystals of the aspartic proteinase endothiapepsin (EC 3.4.23.6) complexed with a potent difluorostatone-containing tripeptide renin inhibitor (CP-81,282). The scissile bond surrogate, an electrophilic ketone, is hydrated in the complex. The pro-(R) (statine-like) hydroxyl of the tetrahedral carbonyl hydrate is hydrogen-bonded to both active-site aspartates 32 and 215 in the position occupied by a water in the native enzyme. The second… CONTINUE READING

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