Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 Å and sequence homology with porcine pepsin
- 1 March 1977
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 266 (5598) , 140-145
- https://doi.org/10.1038/266140a0
Abstract
The polypeptide chain of the acid protease penicillo pepsin folds via an 18-stranded mixed beta-sheet into two distinct lobes separated by a 30-A 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.Keywords
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