1zap
From Proteopedia
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SECRETED ASPARTIC PROTEASE FROM C. ALBICANS
Overview
The three-dimensional structure of a secreted aspartic protease from, Candida albicans complexed with a potent inhibitor reveals variations on, the classical aspartic protease theme that dramatically alter the, specificity of this class of enzymes. The structure presents: (1) an, 8-residue insertion near the first disulfide (Cys 45-Cys 50, pepsin, numbering) that results in a broad flap extending toward the active site;, (2) a 7-residue deletion replacing helix hN2 (Ser 110-Tyr 114), which, enlarges the S3 pocket; (3) a short polar connection between the two rigid, body domains that alters their relative orientation and provides certain, specificity; and (4) an ordered 11-residue addition at the carboxy, terminus. The inhibitor binds in an extended conformation and presents a, branched structure at the P3 position. The implications of these findings, for the design of potent antifungal agents are discussed.
About this Structure
1ZAP is a Single protein structure of sequence from Candida albicans with ZN and A70 as ligands. Active as Candidapepsin, with EC number 3.4.23.24 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure of a secreted aspartic protease from C. albicans complexed with a potent inhibitor: implications for the design of antifungal agents., Abad-Zapatero C, Goldman R, Muchmore SW, Hutchins C, Stewart K, Navaza J, Payne CD, Ray TL, Protein Sci. 1996 Apr;5(4):640-52. PMID:8845753
Page seeded by OCA on Tue Dec 18 18:42:08 2007
