1j71
Structure of the extracellular aspartic proteinase from Candida tropicalis yeast.
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OverviewOverview
The crystal structure of the secreted aspartic proteinase from Candida, tropicalis yeast (SAPT) has been determined to 1.8 A resolution. The, classic aspartic proteinase bilobal structure and domain topology is, conserved in SAPT, with the substrate binding cleft situated between the, two domains. Structural comparisons made with pepsin indicate that, insertions and deletions in the primary sequence modify the SAPT structure, to create a more spacious substrate binding cleft with altered, specificity. An unexpected tetrapeptide has been found to occupy binding, sites S1'-S3', and this suggests the order of release of peptide products, in the catalytic mechanism of these enzymes. Structural features are, considered with regard to previous substrate specificity data.
About this StructureAbout this Structure
1J71 is a Single protein structure of sequence from Candida tropicalis and Unidentified with EOH as ligand. Active as Candidapepsin, with EC number 3.4.23.24 Full crystallographic information is available from OCA.
ReferenceReference
High-resolution structure of the extracellular aspartic proteinase from Candida tropicalis yeast., Symersky J, Monod M, Foundling SI, Biochemistry. 1997 Oct 21;36(42):12700-10. PMID:9335526
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