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| | <StructureSection load='4kf1' size='340' side='right'caption='[[4kf1]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='4kf1' size='340' side='right'caption='[[4kf1]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4kf1]] is a 4 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=4KF1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KF1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4kf1]] is a 4 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=4KF1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KF1 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>, <scene name='pdbligand=HT5:(4S)-4-(DECANOYLAMINO)-5-HYDROXY-3,4-DIHYDRO-2H-THIOPHENIUM'>HT5</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> | + | </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=HT5:(4S)-4-(DECANOYLAMINO)-5-HYDROXY-3,4-DIHYDRO-2H-THIOPHENIUM'>HT5</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vc5|2vc5]], [[2vc7|2vc7]], [[3uf9|3uf9]], [[4ker|4ker]], [[4kes|4kes]], [[4ket|4ket]], [[4keu|4keu]], [[4kev|4kev]], [[4kez|4kez]]</div></td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">php, php SSO2522, SSO2522 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 ATCC 35091])</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=4kf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kf1 OCA], [https://pdbe.org/4kf1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kf1 RCSB], [https://www.ebi.ac.uk/pdbsum/4kf1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kf1 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=4kf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kf1 OCA], [https://pdbe.org/4kf1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kf1 RCSB], [https://www.ebi.ac.uk/pdbsum/4kf1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kf1 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: Chabriere, E]] | + | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Elias, M]] | + | [[Category: Chabriere E]] |
| - | [[Category: Gotthard, G]] | + | [[Category: Elias M]] |
| - | [[Category: Hiblot, J]] | + | [[Category: Gotthard G]] |
| - | [[Category: Hydrolase]]
| + | [[Category: Hiblot J]] |
| - | [[Category: Lactonase]]
| + | |
| Structural highlights
4kf1 is a 4 chain structure with sequence from Saccharolobus solfataricus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | 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
Enzymes are proficient catalysts that enable fast rates of Michaelis-complex formation, the chemical step and products release. These different steps may require different conformational states of the active site that have distinct binding properties. Moreover, the conformational flexibility of the active site mediates alternative, promiscuous functions. Here we focused on the lactonase SsoPox from Sulfolobus solfataricus. SsoPox is a native lactonase endowed with promiscuous phosphotriesterase activity. We identified a position in the active site loop (W263) that governs its flexibility, and thereby affects the substrate specificity of the enzyme. We isolated two different sets of substitutions at position 263 that induce two distinct conformational sampling of the active loop and characterized the structural and kinetic effects of these substitutions. These sets of mutations selectively and distinctly mediate the improvement of the promiscuous phosphotriesterase and oxo-lactonase activities of SsoPox by increasing active-site loop flexibility. These observations corroborate the idea that conformational diversity governs enzymatic promiscuity and is a key feature of protein evolvability.
Differential Active Site Loop Conformations Mediate Promiscuous Activities in the Lactonase SsoPox.,Hiblot J, Gotthard G, Elias M, Chabriere E PLoS One. 2013 Sep 23;8(9):e75272. doi: 10.1371/journal.pone.0075272. PMID:24086491[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
- ↑ Hiblot J, Gotthard G, Elias M, Chabriere E. Differential Active Site Loop Conformations Mediate Promiscuous Activities in the Lactonase SsoPox. PLoS One. 2013 Sep 23;8(9):e75272. doi: 10.1371/journal.pone.0075272. PMID:24086491 doi:http://dx.doi.org/10.1371/journal.pone.0075272
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