6wn0

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==The structure of a CoA-dependent acyl-homoserine lactone synthase, RpaI, with the adduct of SAH and p-coumaroyl CoA==
==The structure of a CoA-dependent acyl-homoserine lactone synthase, RpaI, with the adduct of SAH and p-coumaroyl CoA==
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<StructureSection load='6wn0' size='340' side='right'caption='[[6wn0]]' scene=''>
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<StructureSection load='6wn0' size='340' side='right'caption='[[6wn0]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WN0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6WN0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6wn0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodopseudomonas_palustris Rhodopseudomonas palustris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WN0 FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6wn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wn0 OCA], [http://pdbe.org/6wn0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6wn0 RCSB], [http://www.ebi.ac.uk/pdbsum/6wn0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6wn0 ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=U4Y:(2S)-4-({[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}sulfanyl)-2-{[(2E)-3-(cis-4-hydroxycyclohexa-2,5-dien-1-yl)prop-2-enoyl]amino}butanoic+acid'>U4Y</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6wn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wn0 OCA], [https://pdbe.org/6wn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wn0 RCSB], [https://www.ebi.ac.uk/pdbsum/6wn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wn0 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RPAI_RHOPA RPAI_RHOPA] Catalyzes the synthesis of 4-coumaroyl-homoserine lactone, a quorum-sensing (QS) autoinducer molecule which binds to RpaR transcriptional regulator to regulate expression of QS-dependent genes.<ref>PMID:18563084</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Many bacteria use membrane-diffusible small molecule quorum signals to coordinate gene transcription in response to changes in cell density, known as quorum sensing (QS). Among these, acyl-homoserine lactones (AHL) are wide distributed in Proteobacteria, and are involved in controlling the expression of virulence genes and biofilm formation in pathogens, such as Pseudomonas aeruginosa. AHL molecules are specifically biosynthesized by the cognate LuxI type AHL synthases using S-adenosylmethionine (SAM) and either acyl carrier protein (ACP)- or CoA-coupled fatty acids through a two-step reaction. Here, we characterize a CoA-dependent LuxI synthase from Rhodopseudomonas palustris that utilizes an aryl-CoA substrate that is environmentally derived, specifically p-coumaric acid. We leverage structures of this aryl-CoA-dependent synthase, along with our prior studies of an acyl-CoA synthase, to identify residues that confer substrate chain specificity in these enzymes. We test our predictions by carrying out biochemical, kinetic, and structural characterization of representative AHL signal synthases. Our studies provide an understanding of various AHL synthases that may be deployed in synthetic biological applications and inform on the design of specific small molecule therapeutics that can restrict virulence by targeting quorum signalling.
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Structure-Guided Biochemical Analysis of Quorum Signal Synthase Specificities.,Dong SH, Nhu-Lam M, Nagarajan R, Nair SK ACS Chem Biol. 2020 May 1. doi: 10.1021/acschembio.0c00142. PMID:32356962<ref>PMID:32356962</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6wn0" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Rhodopseudomonas palustris]]
[[Category: Dong S-H]]
[[Category: Dong S-H]]
[[Category: Nair SK]]
[[Category: Nair SK]]

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The structure of a CoA-dependent acyl-homoserine lactone synthase, RpaI, with the adduct of SAH and p-coumaroyl CoA

PDB ID 6wn0

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