4le6: Difference between revisions
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==Crystal structure of the phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenes== | |||
<StructureSection load='4le6' size='340' side='right' caption='[[4le6]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4le6]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_17440 Atcc 17440]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LE6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LE6 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ophc2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=330 ATCC 17440])</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=4le6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4le6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4le6 RCSB], [http://www.ebi.ac.uk/pdbsum/4le6 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
BACKGROUND: Organophosphates (OPs) are neurotoxic compounds for which current methods of elimination are unsatisfactory; thus bio-remediation is considered as a promising alternative. Here we provide the structural and enzymatic characterization of the recently identified enzyme isolated from Pseudomonas pseudoalcaligenes dubbed OPHC2. OPHC2 belongs to the metallo-beta-lactamase superfamily and exhibits an unusual thermal resistance and some OP degrading abilities. PRINCIPAL FINDINGS: The X-ray structure of OPHC2 has been solved at 2.1 A resolution. The enzyme is roughly globular exhibiting a alphabeta/betaalpha topology typical of the metallo-beta-lactamase superfamily. Several structural determinants, such as an extended dimerization surface and an intramolecular disulfide bridge, common features in thermostable enzymes, are consistent with its high Tm (97.8 degrees C). Additionally, we provide the enzymatic characterization of OPHC2 against a wide range of OPs, esters and lactones. SIGNIFICANCE: OPHC2 possesses a broad substrate activity spectrum, since it hydrolyzes various phosphotriesters, esters, and a lactone. Because of its organophosphorus hydrolase activity, and given its intrinsic thermostability, OPHC2 is an interesting candidate for the development of an OPs bio-decontaminant. Its X-ray structure shed light on its active site, and provides key information for the understanding of the substrate binding mode and catalysis. | |||
Structural and Enzymatic Characterization of the Phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenes.,Gotthard G, Hiblot J, Gonzalez D, Elias M, Chabriere E PLoS One. 2013 Nov 4;8(11):e77995. doi: 10.1371/journal.pone.0077995. PMID:24223749<ref>PMID:24223749</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 17440]] | [[Category: Atcc 17440]] | ||
[[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: Alpha beta/beta alpha sandwich]] | [[Category: Alpha beta/beta alpha sandwich]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Metallo-hydrolase]] | [[Category: Metallo-hydrolase]] | ||
[[Category: Phosphotriesterase]] | [[Category: Phosphotriesterase]] | ||
Revision as of 20:33, 21 December 2014
Crystal structure of the phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenesCrystal structure of the phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenes
Structural highlights
Publication Abstract from PubMedBACKGROUND: Organophosphates (OPs) are neurotoxic compounds for which current methods of elimination are unsatisfactory; thus bio-remediation is considered as a promising alternative. Here we provide the structural and enzymatic characterization of the recently identified enzyme isolated from Pseudomonas pseudoalcaligenes dubbed OPHC2. OPHC2 belongs to the metallo-beta-lactamase superfamily and exhibits an unusual thermal resistance and some OP degrading abilities. PRINCIPAL FINDINGS: The X-ray structure of OPHC2 has been solved at 2.1 A resolution. The enzyme is roughly globular exhibiting a alphabeta/betaalpha topology typical of the metallo-beta-lactamase superfamily. Several structural determinants, such as an extended dimerization surface and an intramolecular disulfide bridge, common features in thermostable enzymes, are consistent with its high Tm (97.8 degrees C). Additionally, we provide the enzymatic characterization of OPHC2 against a wide range of OPs, esters and lactones. SIGNIFICANCE: OPHC2 possesses a broad substrate activity spectrum, since it hydrolyzes various phosphotriesters, esters, and a lactone. Because of its organophosphorus hydrolase activity, and given its intrinsic thermostability, OPHC2 is an interesting candidate for the development of an OPs bio-decontaminant. Its X-ray structure shed light on its active site, and provides key information for the understanding of the substrate binding mode and catalysis. Structural and Enzymatic Characterization of the Phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenes.,Gotthard G, Hiblot J, Gonzalez D, Elias M, Chabriere E PLoS One. 2013 Nov 4;8(11):e77995. doi: 10.1371/journal.pone.0077995. PMID:24223749[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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