|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <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://proteopedia.org/fgij/fg.htm?mol=2VC5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vc5]] 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=2VC5 OCA]. For a <b>guided tour on the structure components</b> use [https://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" 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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</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">[[2vc7|2vc7]]</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=2vc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vc5 OCA], [https://pdbe.org/2vc5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vc5 RCSB], [https://www.ebi.ac.uk/pdbsum/2vc5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vc5 ProSAT]</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://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 == |
| - | [[http://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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 35: |
Line 33: |
| | *[[Phosphotriesterase 3D structures|Phosphotriesterase 3D structures]] | | *[[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]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Saccharolobus solfataricus]] | |
| - | [[Category: Aryldialkylphosphatase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chabriere, E]] | + | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Dupuy, J]] | + | [[Category: Chabriere E]] |
| - | [[Category: Elias, M]] | + | [[Category: Dupuy J]] |
| - | [[Category: Lecomte, C]] | + | [[Category: Elias M]] |
| - | [[Category: Manco, G]] | + | [[Category: Lecomte C]] |
| - | [[Category: Mandrich, L]] | + | [[Category: Manco G]] |
| - | [[Category: Masson, P]] | + | [[Category: Mandrich L]] |
| - | [[Category: Merone, L]] | + | [[Category: Masson P]] |
| - | [[Category: Moniot, S]] | + | [[Category: Merone L]] |
| - | [[Category: Rossi, M]] | + | [[Category: Moniot S]] |
| - | [[Category: Biotechnology]]
| + | [[Category: Rossi M]] |
| - | [[Category: Enzyme evolution]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Hyperthermophilic]]
| + | |
| - | [[Category: Lactonase]]
| + | |
| - | [[Category: Phosphotriesterase]]
| + | |
| - | [[Category: Promiscuous activity]]
| + | |
| - | [[Category: Quorum sensing]]
| + | |
| Structural highlights
2vc5 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.
| | Method: | X-ray diffraction, Resolution 2.6Å |
| 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]
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 PubMed
Organophosphates 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
- ↑ 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
- ↑ Elias M, Dupuy J, Merone L, Mandrich L, Porzio E, Moniot S, Rochu D, Lecomte C, Rossi M, Masson P, Manco G, Chabriere E. Structural basis for natural lactonase and promiscuous phosphotriesterase activities. J Mol Biol. 2008 Jun 20;379(5):1017-28. Epub 2008 Apr 16. PMID:18486146 doi:10.1016/j.jmb.2008.04.022
|
