ABSTRACT
The molecular structures of two fungal acid proteases at 3 A resolution have been compared, and found to have similar secondary and tertiary folding. These enzymes are bilobal and have a pronounced cleft between the two lobes. This cleft has been identified as the active site region from inhibitor binding studies. The results of the comparison are discussed in terms of homology among the acid proteases in general.
Subject(s)
Ascomycota/enzymology , Peptide Hydrolases , Rhizopus/enzymology , Xylariales/enzymology , Binding Sites , Gold , Mercury , Models, Structural , Pepsin A , Platinum , Protein Binding , Protein Conformation , Species Specificity , Uranium , X-Ray DiffractionABSTRACT
This paper contains a preliminary report of the crystal structure of the acid protease from Rhizopus chinensis at 2.5 A resolution. The molecule is bilobal with a large cleft between the lobes. Pepstatin binds in the cleft near the catalytically active Asp-35. The overall folding of the molecule consists primarily of antiparallel beta-strands, there being only four small helices.
