1zap
From Proteopedia
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| - | [[Image:1zap.gif|left|200px]]<br /><applet load="1zap" size=" | + | [[Image:1zap.gif|left|200px]]<br /><applet load="1zap" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zap, resolution 2.5Å" /> | caption="1zap, resolution 2.5Å" /> | ||
'''SECRETED ASPARTIC PROTEASE FROM C. ALBICANS'''<br /> | '''SECRETED ASPARTIC PROTEASE FROM C. ALBICANS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ZAP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans] with ZN and A70 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Candidapepsin Candidapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.24 3.4.23.24] Known structural/functional Site: <scene name='pdbsite=ACT:Aspartic Proteinases Are Characterized By Two ASP Residu ...'>ACT</scene>. Full crystallographic information is available from [http:// | + | 1ZAP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=A70:'>A70</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Candidapepsin Candidapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.24 3.4.23.24] Known structural/functional Site: <scene name='pdbsite=ACT:Aspartic+Proteinases+Are+Characterized+By+Two+ASP+Residu+...'>ACT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZAP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: secreted]] | [[Category: secreted]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:22:37 2008'' |
Revision as of 08:22, 3 February 2008
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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 and 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
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