1J71

Structure of the extracellular aspartic proteinase from Candida tropicalis yeast.

Summary for 1J71

• Entry DOI: 10.2210/pdb1j71/pdb
• Related: 1EAG 1ZAP
• Descriptor: Aspartic proteinase, Tetrapeptide Thr-Ile-Thr-Ser, ETHANOL, ... (4 entities in total)
• Functional Keywords: candida tropicalis aspartic protease, sapt1, hydrolase
• Biological source: Candida tropicalis; More
• Cellular location: Secreted: Q00663
• Total number of polymer chains: 2
• Total formula weight: 36651.13

Authors

Symersky, J.,Monod, M.,Foundling, S.I. (deposition date: 2001-05-15, release date: 2001-05-23, Last modification date: 2024-10-16)

Primary citation

Symersky, J.,Monod, M.,Foundling, S.I.
High-resolution structure of the extracellular aspartic proteinase from Candida tropicalis yeast.
Biochemistry, 36:12700-12710, 1997

PubMed Abstract: 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.

PubMed: 9335526
DOI: 10.1021/bi970613x

Experimental method

X-RAY DIFFRACTION (1.8 Å)