1wkr | pdb_00001wkr
Crystal structure of aspartic proteinase from Irpex lacteus
Overview
The crystal structure of Irpex lacteus aspartic proteinase (ILAP) in complex with pepstatin (a six amino acid residue peptide-like inhibitor) was determined at 1.3A resolution. ILAP is a pepsin-like enzyme, widely distributed in nature, with high milk-clotting activity relative to proteolytic activity. The overall structure was in good topological agreement with pepsin and other aspartic proteases. The structure and interaction pattern around the catalytic site were conserved, in agreement with the other aspartic proteinase/inhibitor complex structures reported previously. The high-resolution data also supported the transition state model, as proposed previously for the catalytic mechanism of aspartic proteinase. Unlike the other aspartic proteinases, ILAP was found to require hydrophobic residues either in the P(1) or P(1') site, and also in the P(4) and/or P(3) site(s) for secondary interactions. The inhibitor complex structure also revealed the substrate binding mechanism of ILAP at the P(3) and P(4) site of the substrate, where the inserted loop built up the unique hydrophobic pocket at the P(4) site.
About this Structure
1WKR is a Single protein structure of sequence from Irpex lacteus. Full crystallographic information is available from OCA.
Reference
Crystal structure of aspartic proteinase from Irpex lacteus in complex with inhibitor pepstatin., Fujimoto Z, Fujii Y, Kaneko S, Kobayashi H, Mizuno H, J Mol Biol. 2004 Aug 27;341(5):1227-35. PMID:15321718 Page seeded by OCA on Sat May 3 13:48:58 2008
