1ZAP

SECRETED ASPARTIC PROTEASE FROM C. ALBICANS

Summary for 1ZAP

• Entry DOI: 10.2210/pdb1zap/pdb
• Descriptor: SECRETED ASPARTIC PROTEINASE, ZINC ION, N-ethyl-N-[(4-methylpiperazin-1-yl)carbonyl]-D-phenylalanyl-N-[(1S,2S,4R)-4-(butylcarbamoyl)-1-(cyclohexylmethyl)-2-hyd roxy-5-methylhexyl]-L-norleucinamide, ... (4 entities in total)
• Functional Keywords: aspartic protease, secreted, candida albicans
• Biological source: Candida albicans
• Total number of polymer chains: 1
• Total formula weight: 37126.05

Authors

Abad-Zapatero, C.,Muchmore, S.W. (deposition date: 1996-01-16, release date: 1997-04-21, Last modification date: 2024-10-30)

Primary citation

Abad-Zapatero, C.,Goldman, R.,Muchmore, S.W.,Hutchins, C.,Stewart, K.,Navaza, J.,Payne, C.D.,Ray, T.L.
Structure of a secreted aspartic protease from C. albicans complexed with a potent inhibitor: implications for the design of antifungal agents.
Protein Sci., 5:640-652, 1996

PubMed Abstract: 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.

PubMed: 8845753

Experimental method

X-RAY DIFFRACTION (2.5 Å)