4ybf | pdb_00004ybf

Aspartic Proteinase Sapp2 Secreted from Candida Parapsilosis at 1.25 A Resolution

spinqualitylabelsall models 4ybf, resolution 1.24Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ybf is a 1 chain structure with sequence from Canpc. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PEG Gene: CPAR2_102580 (CANPC) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 A 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. Atomic resolution crystal structure of Sapp2p, a secreted aspartic protease from Candida parapsilosis.,Dostal J, Pecina A, Hruskova-Heidingsfeldova O, Mareckova L, Pichova I, Rezacova P, Lepsik M, Brynda J Acta Crystallogr D Biol Crystallogr. 2015 Dec 1;71(Pt 12):2494-504. doi:, 10.1107/S1399004715019392. Epub 2015 Nov 27. PMID:26627656 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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