Structure of acid protease from Endothia parasitica in cross-linked form at 2.45-A resolution.
The structure of acid protease from Endothia parasitica in strongly cross-linked form is compared with that of the untreated protein at 2.45-a resolution. The only observed conformation change introduced by the cross-linking reaction is at the N terminal. Otherwise the two main chain structures are essentially identical. Approximately 2 molecules of the inhibitor, 1,2-epoxy-3-(p-nitrophenoxy)propane, are found to be incorporated into each protein molecule. They are covalently bound to the two aspartic residues at the active center.
D001203:Ascomycota / Q000201:enzymology*; D008958:Models, Molecular; D010447:Peptide Hydrolases; D011485:Protein Binding; D011487:Protein Conformation; D014961:X-Ray Diffraction; D013098:Xylariales / Q000201:enzymology*
D010447:Peptide Hydrolases