Homology among acid proteases: comparison of crystal structures at 3A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica.
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.
D001203:Ascomycota / Q000201:enzymology*; D001665:Binding Sites; D006046:Gold; D008628:Mercury; D008961:Models, Structural; D010434:Pepsin A; D010447:Peptide Hydrolases; D010984:Platinum; D011485:Protein Binding; D011487:Protein Conformation; D012233:Rhizopus / Q000201:enzymology*; D013045:Species Specificity; D014501:Uranium; D014961:X-Ray Diffraction; D013098:Xylariales / Q000201:enzymology*
D010984:Platinum; D014501:Uranium; D006046:Gold; D010447:Peptide Hydrolases; D010434:Pepsin A; D008628:Mercury