2vc5: Difference between revisions
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==Structural basis for natural lactonase and promiscuous phosphotriesterase activities== | ==Structural basis for natural lactonase and promiscuous phosphotriesterase activities== | ||
<StructureSection load='2vc5' size='340' side='right' caption='[[2vc5]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='2vc5' size='340' side='right'caption='[[2vc5]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2vc5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/'saccharolobus_solfataricus' 'saccharolobus solfataricus']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VC5 OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[2vc5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/'saccharolobus_solfataricus' 'saccharolobus solfataricus']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VC5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VC5 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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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">[[2vc7|2vc7]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vc7|2vc7]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aryldialkylphosphatase Aryldialkylphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.8.1 3.1.8.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aryldialkylphosphatase Aryldialkylphosphatase], with EC number [http://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'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2vc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vc5 OCA], [http://pdbe.org/2vc5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vc5 RCSB], [http://www.ebi.ac.uk/pdbsum/2vc5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vc5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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==See Also== | ==See Also== | ||
*[[Phosphotriesterase|Phosphotriesterase]] | *[[Phosphotriesterase 3D structures|Phosphotriesterase 3D structures]] | ||
*[[Serum Paraoxonase|Serum Paraoxonase]] | *[[Serum Paraoxonase|Serum Paraoxonase]] | ||
*[[SsoPox: a natural lactonase with promiscuous phosphotriesterase activities|SsoPox: a natural lactonase with promiscuous phosphotriesterase activities]] | *[[SsoPox: a natural lactonase with promiscuous phosphotriesterase activities|SsoPox: a natural lactonase with promiscuous phosphotriesterase activities]] | ||
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[[Category: Saccharolobus solfataricus]] | [[Category: Saccharolobus solfataricus]] | ||
[[Category: Aryldialkylphosphatase]] | [[Category: Aryldialkylphosphatase]] | ||
[[Category: Large Structures]] | |||
[[Category: Chabriere, E]] | [[Category: Chabriere, E]] | ||
[[Category: Dupuy, J]] | [[Category: Dupuy, J]] | ||
Revision as of 10:43, 25 June 2020
Structural basis for natural lactonase and promiscuous phosphotriesterase activitiesStructural basis for natural lactonase and promiscuous phosphotriesterase activities
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] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedOrganophosphates are the largest class of known insecticides, several of which are potent nerve agents. Consequently, organophosphate-degrading enzymes are of great scientific interest as bioscavengers and biodecontaminants. Recently, a hyperthermophilic phosphotriesterase (known as SsoPox), from the Archaeon Sulfolobus solfataricus, has been isolated and found to possess a very high lactonase activity. Here, we report the three-dimensional structures of SsoPox in the apo form (2.6 A resolution) and in complex with a quorum-sensing lactone mimic at 2.0 A resolution. The structure also reveals an unexpected active site topology, and a unique hydrophobic channel that perfectly accommodates the lactone substrate. Structural and mutagenesis evidence allows us to propose a mechanism for lactone hydrolysis and to refine the catalytic mechanism established for phosphotriesterases. In addition, SsoPox structures permit the correlation of experimental lactonase and phosphotriesterase activities and this strongly suggests lactonase activity as the cognate function of SsoPox. This example demonstrates that promiscuous activities probably constitute a large and efficient reservoir for the creation of novel catalytic activities. Structural basis for natural lactonase and promiscuous phosphotriesterase activities.,Elias M, Dupuy J, Merone L, Mandrich L, Porzio E, Moniot S, Rochu D, Lecomte C, Rossi M, Masson P, Manco G, Chabriere E J Mol Biol. 2008 Jun 20;379(5):1017-28. Epub 2008 Apr 16. PMID:18486146[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also
References
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