4ker: Difference between revisions
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==Crystal structure of SsoPox W263V== | |||
=== | <StructureSection load='4ker' size='340' side='right' caption='[[4ker]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ker]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KER OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KER FirstGlance]. <br> | |||
==Function== | </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=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]], [[3uf9|3uf9]], [[4kes|4kes]], [[4ket|4ket]], [[4keu|4keu]], [[4kev|4kev]], [[4kez|4kez]], [[4kf1|4kf1]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">php, php SSO2522, SSO2522 ([http://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'>[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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ker FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ker OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ker RCSB], [http://www.ebi.ac.uk/pdbsum/4ker PDBsum]</span></td></tr> | |||
</table> | |||
== 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> | [[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> | ||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:24086491</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aryldialkylphosphatase]] | [[Category: Aryldialkylphosphatase]] | ||
[[Category: Atcc 35091]] | [[Category: Atcc 35091]] | ||
[[Category: Chabriere, E | [[Category: Chabriere, E]] | ||
[[Category: Elias, M | [[Category: Elias, M]] | ||
[[Category: Gotthard, G | [[Category: Gotthard, G]] | ||
[[Category: Hiblot, J | [[Category: Hiblot, J]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Lactonase]] | [[Category: Lactonase]] | ||
Revision as of 09:31, 25 December 2014
Crystal structure of SsoPox W263VCrystal structure of SsoPox W263V
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 PubMedEnzymes 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. References
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