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| | <StructureSection load='5vrk' size='340' side='right'caption='[[5vrk]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='5vrk' size='340' side='right'caption='[[5vrk]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5vrk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VRK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VRK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5vrk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VRK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VRK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.4Å</td></tr> |
| - | <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>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[5vri|5vri]], [[5vsa|5vsa]], [[5w3u|5w3u]], [[5w3w|5w3w]], [[5w3z|5w3z]]</div></td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aryldialkylphosphatase Aryldialkylphosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.8.1 3.1.8.1] </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=5vrk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vrk OCA], [https://pdbe.org/5vrk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vrk RCSB], [https://www.ebi.ac.uk/pdbsum/5vrk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vrk 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=5vrk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vrk OCA], [https://pdbe.org/5vrk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vrk RCSB], [https://www.ebi.ac.uk/pdbsum/5vrk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vrk ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PHP_SULSO PHP_SULSO]] Has a low paraoxonase activity. Also active, but with a lower activity, against other oregano-phosphorus insecticides such as Dursban, Coumaphos, pNP-butanoate or parathion.<ref>PMID:15909078</ref>
| + | [https://www.uniprot.org/uniprot/PHP_SACS2 PHP_SACS2] Has a low paraoxonase activity. Also active, but with a lower activity, against other organo-phosphorus insecticides such as Dursban, Coumaphos, pNP-butanoate or parathion.<ref>PMID:15909078</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aryldialkylphosphatase]] | |
| - | [[Category: Atcc 35091]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bergonzi, C]] | + | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Chabriere, E]] | + | [[Category: Bergonzi C]] |
| - | [[Category: Daude, D]] | + | [[Category: Chabriere E]] |
| - | [[Category: Elias, M]] | + | [[Category: Daude D]] |
| - | [[Category: Gotthard, G]] | + | [[Category: Elias M]] |
| - | [[Category: Hiblot, J]] | + | [[Category: Gotthard G]] |
| - | [[Category: Jacquet, P]] | + | [[Category: Hiblot J]] |
| - | [[Category: Hydrolase]]
| + | [[Category: Jacquet P]] |
| - | [[Category: Insecticides]]
| + | |
| - | [[Category: Lactonase]]
| + | |
| - | [[Category: Mutant]]
| + | |
| - | [[Category: Organophosphate]]
| + | |
| - | [[Category: Organophosphorous]]
| + | |
| - | [[Category: Phosphotriesterase]]
| + | |
| - | [[Category: Quorum sensing]]
| + | |
| Structural highlights
5vrk is a 2 chain structure with sequence from Saccharolobus solfataricus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.4Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
PHP_SACS2 Has a low paraoxonase activity. Also active, but with a lower activity, against other organo-phosphorus insecticides such as Dursban, Coumaphos, pNP-butanoate or parathion.[1]
Publication Abstract from PubMed
The redesign of enzyme active sites to alter their function or specificity is a difficult yet appealing challenge. Here we used a structure-based design approach to engineer the lactonase SsoPox from Sulfolobus solfataricus into a phosphotriesterase. The five best variants were characterized and their structure was solved. The most active variant, alphasD6 (V27A-Y97W-L228M-W263M) demonstrates a large increase in catalytic efficiencies over the wild-type enzyme, with increases of 2,210-fold, 163-fold, 58-fold, 16-fold against methyl-parathion, malathion, ethyl-paraoxon, and methyl-paraoxon, respectively. Interestingly, the best mutants are also capable of degrading fensulfothion, which is reported to be an inhibitor for the wild-type enzyme, as well as others that are not substrates of the starting template or previously reported W263 mutants. The broad specificity of these engineered variants makes them promising candidates for the bioremediation of organophosphorus compounds. Analysis of their structures reveals that the increase in activity mainly occurs through the destabilization of the active site loop involved in substrate binding, and it has been observed that the level of disorder correlates with the width of the enzyme specificity spectrum. This finding supports the idea that active site conformational flexibility is essential to the acquisition of broader substrate specificity.
Rational engineering of a native hyperthermostable lactonase into a broad spectrum phosphotriesterase.,Jacquet P, Hiblot J, Daude D, Bergonzi C, Gotthard G, Armstrong N, Chabriere E, Elias M Sci Rep. 2017 Dec 1;7(1):16745. doi: 10.1038/s41598-017-16841-0. PMID:29196634[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Merone L, Mandrich L, Rossi M, Manco G. A thermostable phosphotriesterase from the archaeon Sulfolobus solfataricus: cloning, overexpression and properties. Extremophiles. 2005 Aug;9(4):297-305. Epub 2005 May 21. PMID:15909078 doi:10.1007/s00792-005-0445-4
- ↑ Jacquet P, Hiblot J, Daude D, Bergonzi C, Gotthard G, Armstrong N, Chabriere E, Elias M. Rational engineering of a native hyperthermostable lactonase into a broad spectrum phosphotriesterase. Sci Rep. 2017 Dec 1;7(1):16745. doi: 10.1038/s41598-017-16841-0. PMID:29196634 doi:http://dx.doi.org/10.1038/s41598-017-16841-0
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