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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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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DOI: https://doi.org/10.1038/266140a0
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