Structural highlights
Function
CARP_CANTR
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Symersky J, Monod M, Foundling SI. High-resolution structure of the extracellular aspartic proteinase from Candida tropicalis yeast. Biochemistry. 1997 Oct 21;36(42):12700-10. PMID:9335526 doi:http://dx.doi.org/10.1021/bi970613x
