5w8c

<StructureSection load='5w8c' size='340' side='right' caption='[[5w8c]], [[Resolution|resolution]] 1.85&Aring;' scene=''>

<table><tr><td colspan='2'>[[5w8c]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W8C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W8C FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IVC:ISOVALERYL-COENZYME+A'>IVC</scene>, <scene name='pdbligand=MTA:5-DEOXY-5-METHYLTHIOADENOSINE'>MTA</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5w8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w8c OCA], [http://pdbe.org/5w8c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w8c RCSB], [http://www.ebi.ac.uk/pdbsum/5w8c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w8c ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

In several Proteobacteria, LuxI-type enzymes catalyze the biosynthesis of acyl-homoserine lactones (AHL) signals using S-adenosyl-l-methionine and either cellular acyl carrier protein (ACP)-coupled fatty acids or CoA-aryl/acyl moieties as progenitors. Little is known about the molecular mechanism of signal biosynthesis, the basis for substrate specificity, or the rationale for donor specificity for any LuxI member. Here, we present several cocrystal structures of BjaI, a CoA-dependent LuxI homolog that represent views of enzyme complexes that exist along the reaction coordinate of signal synthesis. Complementary biophysical, structure-function, and kinetic analysis define the features that facilitate the unusual acyl conjugation with S-adenosylmethionine (SAM). We also identify the determinant that establishes specificity for the acyl donor and identify residues that are critical for acyl/aryl specificity. These results highlight how a prevalent scaffold has evolved to catalyze quorum signal synthesis and provide a framework for the design of small-molecule antagonists of quorum signaling.

Molecular basis for the substrate specificity of quorum signal synthases.,Dong SH, Frane ND, Christensen QH, Greenberg EP, Nagarajan R, Nair SK Proc Natl Acad Sci U S A. 2017 Aug 22;114(34):9092-9097. doi:, 10.1073/pnas.1705400114. Epub 2017 Aug 7. PMID:28784791<ref>PMID:28784791</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 5w8c" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Dong, S H]]

[[Category: Nair, S K]]

[[Category: Acyl-homoserine lactone]]

[[Category: Biosynthetic protein]]

[[Category: Coenzyme some]]