View source for 3ufa


==Crystal structure of the staphylococcal serine protease SplA in complex with a specific phosphonate inhibitor==
<StructureSection load='3ufa' size='340' side='right'caption='[[3ufa]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ufa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_NCTC_8325 Staphylococcus aureus subsp. aureus NCTC 8325]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UFA 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=VPF:N-(3-CARBOXYPROPANOYL)-L-VALYL-N-[(1S)-2-PHENYL-1-PHOSPHONOETHYL]-L-PROLINAMIDE'>VPF</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=3ufa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ufa OCA], [https://pdbe.org/3ufa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ufa RCSB], [https://www.ebi.ac.uk/pdbsum/3ufa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ufa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SPLA_STAA8 SPLA_STAA8] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Staphylococcus aureus is responsible for a variety of human infections, including life-threatening, systemic conditions. Secreted proteome, including a range of proteases, constitutes the major virulence factor of the bacterium. However, the functions of individual enzymes, in particular SplA protease, remain poorly characterized. Here, we report development of specific inhibitors of SplA protease. The design, synthesis, and activity of a series of alpha-aminoalkylphosphonate diaryl esters and their peptidyl derivatives are described. Potent inhibitors of SplA are reported, which may facilitate future investigation of physiological function of the protease. The binding modes of the high-affinity compounds Cbz-PheP -(OC6 H4 -4-SO2 CH3 )2 and Suc-Val-Pro-PheP -(OC6 H5 )2 are revealed by high-resolution crystal structures of complexes with the protease. Surprisingly, the binding mode of both compounds deviates from previously characterized canonical interaction of alpha-aminoalkylphosphonate peptidyl derivatives and family S1 serine proteases.

Development and binding characteristics of phosphonate inhibitors of SplA protease from Staphylococcus aureus.,Burchacka E, Zdzalik M, Niemczyk JS, Pustelny K, Popowicz G, Wladyka B, Dubin A, Potempa J, Sienczyk M, Dubin G, Oleksyszyn J Protein Sci. 2013 Dec 4. doi: 10.1002/pro.2403. PMID:24375505<ref>PMID:24375505</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ufa" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus subsp. aureus NCTC 8325]]
[[Category: Dubin G]]
[[Category: Oleksyszyn J]]
[[Category: Pietrusewicz E]]
[[Category: Popowicz GM]]
[[Category: Potempa J]]
[[Category: Pustelny K]]
[[Category: Stec-Niemczyk J]]
[[Category: Zdzalik M]]