title: Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 A and sequence homology with porcine pepsin.
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.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003461:Crystallography; D010450:Endopeptidases; D008958:Models, Molecular; D010407:Penicillium / Q000201:enzymology*; D010434:Pepsin A; D011487:Protein Conformation; D013552:Swine; D014961:X-Ray Diffraction
chemical_list: D010450:Endopeptidases; D010434:Pepsin A