3uf9: Difference between revisions
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==Crystal structure of SsoPox in complex with the phosphotriester fensulfothion== | ==Crystal structure of SsoPox in complex with the phosphotriester fensulfothion== | ||
<StructureSection load='3uf9' size='340' side='right' caption='[[3uf9]], [[Resolution|resolution]] 2.68Å' scene=''> | <StructureSection load='3uf9' size='340' side='right'caption='[[3uf9]], [[Resolution|resolution]] 2.68Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3uf9]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3uf9]] 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=3UF9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UF9 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=FST:O,O-DIETHYL+O-{4-[(R)-METHYLSULFINYL]PHENYL}+PHOSPHOROTHIOATE'>FST</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=FST:O,O-DIETHYL+O-{4-[(R)-METHYLSULFINYL]PHENYL}+PHOSPHOROTHIOATE'>FST</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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='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">[[2vc5|2vc5]], [[2vc7|2vc7]]</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]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">php, SSO2522 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">php, 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'>[ | <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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3uf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uf9 OCA], [https://pdbe.org/3uf9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uf9 RCSB], [https://www.ebi.ac.uk/pdbsum/3uf9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uf9 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> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 24: | Line 24: | ||
==See Also== | ==See Also== | ||
*[[Phosphotriesterase|Phosphotriesterase]] | *[[Phosphotriesterase 3D structures|Phosphotriesterase 3D structures]] | ||
*[[Serum Paraoxonase|Serum Paraoxonase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 31: | Line 32: | ||
[[Category: Aryldialkylphosphatase]] | [[Category: Aryldialkylphosphatase]] | ||
[[Category: Atcc 35091]] | [[Category: Atcc 35091]] | ||
[[Category: Large Structures]] | |||
[[Category: Chabriere, E]] | [[Category: Chabriere, E]] | ||
[[Category: Elias, M]] | [[Category: Elias, M]] | ||
Revision as of 09:10, 13 July 2022
Crystal structure of SsoPox in complex with the phosphotriester fensulfothionCrystal structure of SsoPox in complex with the phosphotriester fensulfothion
Structural highlights
Function[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.[1] Publication Abstract from PubMedSsoPox is a lactonase endowed with promiscuous phosphotriesterase activity isolated from Sulfolobus solfataricus that belongs to the Phosphotriesterase-Like Lactonase family. Because of its intrinsic thermal stability, SsoPox is seen as an appealing candidate as a bioscavenger for organophosphorus compounds. A comprehensive kinetic characterisation of SsoPox has been performed with various phosphotriesters (insecticides) and phosphodiesters (nerve agent analogues) as substrates. We show that SsoPox is active for a broad range of OPs and remains active under denaturing conditions. In addition, its OP hydrolase activity is highly stimulated by anionic detergent at ambient temperature and exhibits catalytic efficiencies as high as k(cat)/K(M) of 10(5) M(-1)s(-1) against a nerve agent analogue. The structure of SsoPox bound to the phosphotriester fensulfothion reveals an unexpected and non-productive binding mode. This feature suggests that SsoPox's active site is sub-optimal for phosphotriester binding, which depends not only upon shape but also on localised charge of the ligand. Characterisation of the organophosphate hydrolase catalytic activity of SsoPox.,Hiblot J, Gotthard G, Chabriere E, Elias M Sci Rep. 2012;2:779. doi: 10.1038/srep00779. Epub 2012 Nov 8. PMID:23139857[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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