View source for 4ng2


==Crystal structure of LasR LBD-QslA complex from Pseudomonas aeruginosa==
<StructureSection load='4ng2' size='340' side='right'caption='[[4ng2]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ng2]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NG2 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]] 2.413&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OHN:N-3-OXO-DODECANOYL-L-HOMOSERINE+LACTONE'>OHN</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=4ng2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ng2 OCA], [https://pdbe.org/4ng2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ng2 RCSB], [https://www.ebi.ac.uk/pdbsum/4ng2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ng2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LASR_PSEAE LASR_PSEAE] Transcriptional activator of elastase structural gene (LasB). Binds to the PAI autoinducer.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The human pathogen Pseudomonas aeruginosa coordinates the expression of virulence factors by using quorum sensing (QS), a signaling cascade triggered by the QS signal molecule and its receptor, a member of the LuxR family of QS transcriptional factors (LasR). The QS threshold and response in P. aeruginosa is defined by a QS LasR-specific antiactivator (QslA), which binds to LasR and prevents it from binding to its target promoter. However, how QslA binds to LasR and regulates its DNA binding activity in QS remains elusive. Here we report the crystal structure of QslA in complex with the N-terminal ligand binding domain of LasR. QsIA exists as a functional dimer to interact with the LasR ligand binding domain. Further analysis shows that QsIA binding occupies the LasR dimerization interface and consequently disrupts LasR dimerization, thereby preventing LasR from binding to its target DNA and disturbing normal QS. Our findings provide a structural model for understanding the QslA-mediated antiactivation mechanism in QS through protein-protein interaction.

QsIA disrupts LasR dimerization in antiactivation of bacterial quorum sensing.,Fan H, Dong Y, Wu D, Bowler MW, Zhang L, Song H Proc Natl Acad Sci U S A. 2013 Dec 6. PMID:24319092<ref>PMID:24319092</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ng2" style="background-color:#fffaf0;"></div>

==See Also==
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Fan H]]
[[Category: Song H]]
[[Category: Wu DH]]