2h6t: Difference between revisions
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'''Secreted aspartic proteinase (Sap) 3 from Candida albicans complexed with pepstatin A''' | '''Secreted aspartic proteinase (Sap) 3 from Candida albicans complexed with pepstatin A''' | ||
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[[Category: Maskos, K.]] | [[Category: Maskos, K.]] | ||
[[Category: Ruge, E.]] | [[Category: Ruge, E.]] | ||
[[Category: | [[Category: Aspartic proteinase]] | ||
[[Category: | [[Category: Hydrolase]] | ||
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Revision as of 05:56, 4 May 2008
Secreted aspartic proteinase (Sap) 3 from Candida albicans complexed with pepstatin A
OverviewOverview
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.
About this StructureAbout this Structure
2H6T is a Single protein structure of sequence from Candida albicans. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Sun May 4 05:56:12 2008