View source for 4ybf


==Aspartic Proteinase Sapp2 Secreted from Candida Parapsilosis at 1.25 A Resolution==
<StructureSection load='4ybf' size='340' side='right'caption='[[4ybf]], [[Resolution|resolution]] 1.24&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ybf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_parapsilosis_CDC317 Candida parapsilosis CDC317]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YBF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YBF FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.24&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ybf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ybf OCA], [https://pdbe.org/4ybf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ybf RCSB], [https://www.ebi.ac.uk/pdbsum/4ybf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ybf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G8B6Y8_CANPC G8B6Y8_CANPC] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:26627656</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ybf" style="background-color:#fffaf0;"></div>

==See Also==
*[[Proteinase 3D structures|Proteinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Candida parapsilosis CDC317]]
[[Category: Large Structures]]
[[Category: Brynda J]]
[[Category: Dostal J]]
[[Category: Hruskova-Heidingsfeldova O]]
[[Category: Mareckova L]]
[[Category: Pichova I]]
[[Category: Rezacova P]]