1zap
From Proteopedia
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| , resolution 2.5Å | |||||||
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| Sites: | |||||||
| Ligands: | and | ||||||
| Activity: | Candidapepsin, with EC number 3.4.23.24 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Thu Mar 20 15:33:17 2008
