2H6T
Secreted aspartic proteinase (Sap) 3 from Candida albicans complexed with pepstatin A
Summary for 2H6T
| Entry DOI | 10.2210/pdb2h6t/pdb |
| Related | 2H6S |
| Related PRD ID | PRD_000557 |
| Descriptor | Candidapepsin-3, pepstatin A, ZINC ION, ... (4 entities in total) |
| Functional Keywords | aspartic proteinase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Candida albicans More |
| Total number of polymer chains | 2 |
| Total formula weight | 37293.13 |
| Authors | Ruge, E.,Borelli, C.,Maskos, K.,Huber, R. (deposition date: 2006-06-01, release date: 2007-06-12, Last modification date: 2024-10-30) |
| Primary citation | Borelli, C.,Ruge, E.,Schaller, M.,Monod, M.,Korting, H.C.,Huber, R.,Maskos, K. The crystal structure of the secreted aspartic proteinase 3 from Candida albicans and its complex with pepstatin A. Proteins, 68:738-748, 2007 Cited by PubMed Abstract: 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. PubMed: 17510964DOI: 10.1002/prot.21425 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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