http://www.cnr.it/ontology/cnr/individuo/prodotto/ID8924
Structural basis for natural lactonase and promiscuous phosphotriesterase activities (Articolo in rivista)
- Type
- 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
- 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)
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- 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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