3uf9: Difference between revisions

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<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=3uf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uf9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uf9 RCSB], [http://www.ebi.ac.uk/pdbsum/3uf9 PDBsum]</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=3uf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uf9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uf9 RCSB], [http://www.ebi.ac.uk/pdbsum/3uf9 PDBsum]</span></td></tr>
</table>
</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> 
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 10:25, 24 December 2014

Crystal structure of SsoPox in complex with the phosphotriester fensulfothionCrystal structure of SsoPox in complex with the phosphotriester fensulfothion

Structural highlights

3uf9 is a 4 chain structure with sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
NonStd Res:
Gene:php, SSO2522 (Sulfolobus solfataricus)
Activity:Aryldialkylphosphatase, with EC number 3.1.8.1
Resources:FirstGlance, OCA, RCSB, PDBsum

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 PubMed

SsoPox 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.

References

  1. 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
  2. Hiblot J, Gotthard G, Chabriere E, Elias M. Characterisation of the organophosphate hydrolase catalytic activity of SsoPox. Sci Rep. 2012;2:779. doi: 10.1038/srep00779. Epub 2012 Nov 8. PMID:23139857 doi:10.1038/srep00779

3uf9, resolution 2.68Å

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