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Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 Å and sequence homology with porcine pepsin

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Abstract

The polypeptide chain of the acid protease penicillopepsin folds via an 18-stranded mixed β-sheet into two distinct lobes separated by a 30-Å long groove which is the extended substrate binding site. The catalytic residues Asp-32 and Asp-215 are located in this groove and their carboxyl groups are in intimate contact. Alignment of the amino acid sequence with that of pepsin shows regions of high homology.

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Authors and Affiliations

  1. MRC Group on Protein Structure and Function, University of Alberta, Edmonton, Alberta, T6G 2H7, Canada

    I-Nan Hsu, Louis T. J. Delbaere & Michael N. G. James

  2. Department of Biochemistry, University of Toronto, Toronto, M5S 1A8, Canada

    Theo Hofmann

Authors
  1. I-Nan Hsu
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  2. Louis T. J. Delbaere
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  3. Michael N. G. James
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  4. Theo Hofmann
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Hsu, IN., Delbaere, L., James, M. et al. Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 Å and sequence homology with porcine pepsin. Nature 266, 140–145 (1977). https://doi.org/10.1038/266140a0

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