2h6t

Secreted aspartic proteinase (Sap) 3 from Candida albicans complexed with pepstatin A

spinqualitylabelsall models 2h6t, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2h6t is a 2 chain structure with sequence from Candida albicans and Streptomyces argenteolus subsp. toyonakensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: IVA, STA, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CARP3_CANAL Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The family of secreted aspartic proteinases (Sap) encoded by 10 SAP genes is an important virulence factor during Candida albicans (C. albicans) infections. Antagonists to Saps could be envisioned to help prevent or treat candidosis in immunocompromised patients. The knowledge of several Sap structures is crucial for inhibitor design; only the structure of Sap2 is known. We report the 1.9 and 2.2 A resolution X-ray crystal structures of Sap3 in a stable complex with pepstatin A and in the absence of an inhibitor, shedding further light on the enzyme inhibitor binding. Inhibitor binding causes active site closure by the movement of a flap segment. Comparison of the structures of Sap3 and Sap2 identifies elements responsible for the specificity of each isoenzyme. The crystal structure of the secreted aspartic proteinase 3 from Candida albicans and its complex with pepstatin A.,Borelli C, Ruge E, Schaller M, Monod M, Korting HC, Huber R, Maskos K Proteins. 2007 Aug 15;68(3):738-48. PMID:17510964 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pepsin

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