View source for 4aky


==CRYSTAL STRUCTURE OF VIRB8 FROM BRUCELLA SUIS IN COMPLEX WITH INTERACTION INHIBITOR 2-(butylamino)-8-quinolinol==
<StructureSection load='4aky' size='340' side='right'caption='[[4aky]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4aky]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Brucella_suis Brucella suis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AKY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AKY 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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4LL:2-(BUTYLAMINO)QUINOLIN-8-OL'>4LL</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=4aky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aky OCA], [https://pdbe.org/4aky PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aky RCSB], [https://www.ebi.ac.uk/pdbsum/4aky PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aky ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VIRB8_BRUSU VIRB8_BRUSU] The VirB system could be required for the establishment of the replication niche in the host.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Secretion systems translocate virulence factors of many bacterial pathogens, enabling their survival inside the host organism. Consequently, inhibition strongly attenuates pathogenicity and can be considered a target for novel antimicrobial drugs. The type IV secretion system (T4SS) of the intracellular pathogen Brucella is a prerequisite for its virulence, and in this work we targeted the interactions of the essential assembly factor protein, VirB8, using small-molecule inhibitors. High-throughput screening identified several potent and specific inhibitors, and the target-binding site of these inhibitors was identified by X-ray crystallography, in silico docking, and analysis of the derivates of the inhibitor B8I-2. VirB8 interaction inhibitors bind to a surface groove opposite to the dimerization interface, and by varying the binding-site residues, we were able to determine which residues are required for inhibitor activity. E115 and K182 were found to be especially important, and changes at R114, Y229, and L151 also reduced inhibitor efficiency.

Identification of the Binding Site of Brucella VirB8 Interaction Inhibitors.,Smith MA, Coincon M, Paschos A, Jolicoeur B, Lavallee P, Sygusch J, Baron C Chem Biol. 2012 Aug 24;19(8):1041-8. PMID:22921071<ref>PMID:22921071</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4aky" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Brucella suis]]
[[Category: Large Structures]]
[[Category: Baron C]]
[[Category: Coincon M]]
[[Category: Smith MA]]
[[Category: Sygusch J]]