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 ... [(full description)]
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]. Structure known Active Site: ACT. 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
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