4Y9W

Aspartic Proteinase Sapp2 Secreted from Candida Parapsilosis at 0.82 A Resolution.

Summary for 4Y9W

• Entry DOI: 10.2210/pdb4y9w/pdb
• Related: 3FV3
• Related PRD ID: PRD_000557
• Descriptor: Aspartic acid endopeptidase Sapp2, PEPTIDE (3 entities in total)
• Functional Keywords: candidapepsin, aspartic acid endopeptidase, hydrolase
• Biological source: Candida parapsilosis (Yeast); More
• Total number of polymer chains: 2
• Total formula weight: 36160.88

Authors

Dostal, J.,Brynda, J.,Hruskova-Heidingsfeldova, O.,Rezacova, P.,Mareckova, L.,Pichova, I. (deposition date: 2015-02-17, release date: 2016-11-30, Last modification date: 2024-11-13)

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

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: 26627656
DOI: 10.1107/S1399004715019392

Experimental method

X-RAY DIFFRACTION (0.83 Å)