Structural basis for natural lactonase and promiscuous phosphotriesterase activities (Articolo in rivista)

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Label
  • Structural basis for natural lactonase and promiscuous phosphotriesterase activities (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.jmb.2008.04.022 (literal)
Alternative label
  • Elias M.; Dupuy J.; Merone L.; Mandrich L.; Porzio E.; Moniot S.; Rochu d.; Lecomte C.; Rossi M.; Masson P.; Manco G.; Chabriere E. (2008)
    Structural basis for natural lactonase and promiscuous phosphotriesterase activities
    in Journal of Molecular Biology
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Elias M.; Dupuy J.; Merone L.; Mandrich L.; Porzio E.; Moniot S.; Rochu d.; Lecomte C.; Rossi M.; Masson P.; Manco G.; Chabriere E. (literal)
Pagina inizio
  • 1017 (literal)
Pagina fine
  • 1028 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 379 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 5 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • CNR, Ist Biochim Proteine, I-80131 Naples, Italy Univ Henri Poincare, CNRS, Lab Cristallog & Modelisat Mat Mineraux & Biol, F-54506 Nancy, France Univ Aix Marseille 2, CNRS, F-13288 Marseille, France Inst Biol Struct JP EBEL, Lab Cristallogenese & Cristallog Proteines, F-38027 Grenoble, France CNR, Ist Biochim Proteine, I-80131 Naples, Italy Ctr Rech Serv Sante Armees, Unite Enzymol, Dept Toxicol, F-38702 La Tronche, France E-mail Address: g.manco@ibp.cnr.it, eric.chabriere@afmb.univ-mrs.fr (literal)
Titolo
  • Structural basis for natural lactonase and promiscuous phosphotriesterase activities (literal)
Abstract
  • 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 Å resolution) and in complex with a quorum-sensing lactone mimic at 2.0 Å 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. (literal)
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