4YBF
Aspartic Proteinase Sapp2 Secreted from Candida Parapsilosis at 1.25 A Resolution
Summary for 4YBF
| Entry DOI | 10.2210/pdb4ybf/pdb |
| Descriptor | Candidapepsin-2, DI(HYDROXYETHYL)ETHER (3 entities in total) |
| Functional Keywords | aspartic proteinase sapp2, hydrolase |
| Biological source | Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 35580.13 |
| Authors | Dostal, J.,Hruskova-Heidingsfeldova, O.,Rezacova, P.,Brynda, J.,Mareckova, L.,Pichova, I. (deposition date: 2015-02-18, release date: 2016-01-27, Last modification date: 2024-11-20) |
| Primary citation | Dostal, J.,Pecina, A.,Hruskova-Heidingsfeldova, O.,Mareckova, L.,Pichova, I.,Rezacova, P.,Lepsik, M.,Brynda, J. Atomic resolution crystal structure of Sapp2p, a secreted aspartic protease from Candida parapsilosis. Acta Crystallogr.,Sect.D, 71:2494-2504, 2015 Cited by PubMed Abstract: The virulence of the Candida pathogens is enhanced by the production of secreted aspartic proteases, which therefore represent possible targets for drug design. Here, the crystal structure of the secreted aspartic protease Sapp2p from Candida parapsilosis was determined. Sapp2p was isolated from its natural source and crystallized in complex with pepstatin A, a classical aspartic protease inhibitor. The atomic resolution of 0.83 Å allowed the protonation states of the active-site residues to be inferred. A detailed comparison of the structure of Sapp2p with the structure of Sapp1p, the most abundant C. parapsilosis secreted aspartic protease, was performed. The analysis, which included advanced quantum-chemical interaction-energy calculations, uncovered molecular details that allowed the experimentally observed equipotent inhibition of both isoenzymes by pepstatin A to be rationalized. PubMed: 26627656DOI: 10.1107/S1399004715019392 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.24 Å) |
Structure validation
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