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3ojg

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Current revision (11:16, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3ojg' size='340' side='right'caption='[[3ojg]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='3ojg' size='340' side='right'caption='[[3ojg]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ojg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_kaustophilus"_prickett_1928 "bacillus kaustophilus" prickett 1928]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OJG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ojg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_kaustophilus Geobacillus kaustophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OJG FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HL4:N-[(3S)-2-OXOTETRAHYDROFURAN-3-YL]BUTANAMIDE'>HL4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 1.6&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></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=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HL4:N-[(3S)-2-OXOTETRAHYDROFURAN-3-YL]BUTANAMIDE'>HL4</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GK1506 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1462 "Bacillus kaustophilus" Prickett 1928])</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=3ojg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ojg OCA], [https://pdbe.org/3ojg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ojg RCSB], [https://www.ebi.ac.uk/pdbsum/3ojg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ojg ProSAT]</span></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=3ojg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ojg OCA], [https://pdbe.org/3ojg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ojg RCSB], [https://www.ebi.ac.uk/pdbsum/3ojg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ojg ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q5KZU5_GEOKA Q5KZU5_GEOKA]
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A thermostable quorum-quenching lactonase from Geobacillus kaustophilus HTA426 (GI: 56420041) was used as an initial template for in vitro directed evolution experiments. This enzyme belongs to the phosphotriesterase-like lactonase (PLL) group of enzymes within the amidohydrolase superfamily that hydrolyze N-acylhomoserine lactones (AHLs) that are involved in virulence pathways of quorum-sensing pathogenic bacteria. Here we have determined the N-butyryl-L-homoserine lactone-liganded structure of the catalytically inactive D266N mutant of this enzyme to a resolution of 1.6 A. Using a tunable, bioluminescence-based quorum-quenching molecular circuit, the catalytic efficiency was enhanced, and the AHL substrate range increased through two point mutations on the loops at the C-terminal ends of the third and seventh beta-strands. This E101N/R230I mutant had an increased value of k(cat)/K(m) of 72-fold toward 3-oxo-N-dodecanoyl-L-homoserine lactone. The evolved mutant also exhibited lactonase activity toward N-butyryl-L-homoserine lactone, an AHL that was previously not hydrolyzed by the wild-type enzyme. Both the purified wild-type and mutant enzymes contain a mixture of zinc and iron and are colored purple and brown, respectively, at high concentrations. The origin of this coloration is suggested to be because of a charge transfer complex involving the beta-cation and Tyr-99 within the enzyme active site. Modulation of the charge transfer complex alters the lactonase activity of the mutant enzymes and is reflected in enzyme coloration changes. We attribute the observed enhancement in catalytic reactivity of the evolved enzyme to favorable modulations of the active site architecture toward productive geometries required for chemical catalysis.
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Directed evolution of a thermostable quorum-quenching lactonase from the amidohydrolase superfamily.,Chow JY, Xue B, Lee KH, Tung A, Wu L, Robinson RC, Yew WS J Biol Chem. 2010 Dec 24;285(52):40911-20. Epub 2010 Oct 27. PMID:20980257<ref>PMID:20980257</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 3ojg" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Phosphotriesterase 3D structures|Phosphotriesterase 3D structures]]
*[[Phosphotriesterase 3D structures|Phosphotriesterase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus kaustophilus prickett 1928]]
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[[Category: Geobacillus kaustophilus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chow, J Y]]
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[[Category: Chow JY]]
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[[Category: Robinson, R C]]
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[[Category: Robinson RC]]
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[[Category: Tung, A]]
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[[Category: Tung A]]
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[[Category: Xue, B]]
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[[Category: Xue B]]
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[[Category: Hydrolase]]
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[[Category: Lactonase]]
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Current revision

Structure of an inactive lactonase from Geobacillus kaustophilus with bound N-butyryl-DL-homoserine lactone

PDB ID 3ojg

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