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==The structure of a COA-dependent acyl-homoserine lactone synthase, BjaI, with SAM and isopentyl-CoA==
==The structure of a COA-dependent acyl-homoserine lactone synthase, BjaI, with SAM and isopentyl-CoA==
<StructureSection load='5w8a' size='340' side='right' caption='[[5w8a]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='5w8a' size='340' side='right'caption='[[5w8a]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5w8a]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W8A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W8A FirstGlance]. <br>
<table><tr><td colspan='2'>[[5w8a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bradyrhizobium_japonicum Bradyrhizobium japonicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W8A FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A1S:isopentyl-Coenzyme+A'>A1S</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
</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&#8491;</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=5w8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w8a OCA], [http://pdbe.org/5w8a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w8a RCSB], [http://www.ebi.ac.uk/pdbsum/5w8a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w8a ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1S:isopentyl-Coenzyme+A'>A1S</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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=5w8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w8a OCA], [https://pdbe.org/5w8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w8a RCSB], [https://www.ebi.ac.uk/pdbsum/5w8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w8a ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== 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>
</div>
<div class="pdbe-citations 5w8a" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Dong, S H]]
[[Category: Bradyrhizobium japonicum]]
[[Category: Nair, S K]]
[[Category: Large Structures]]
[[Category: Acyl-homoserine lactone]]
[[Category: Dong S-H]]
[[Category: Biosynthetic protein]]
[[Category: Nair SK]]
[[Category: Bjai]]
[[Category: Coenzyme some]]

Latest revision as of 14:14, 13 March 2024

The structure of a COA-dependent acyl-homoserine lactone synthase, BjaI, with SAM and isopentyl-CoA

5w8a, resolution 2.00Å

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