Structural determinants of the high thermal stability of SsoPox from the hyperthermophilic archaeon Sulfolobus solfataricus. (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Structural determinants of the high thermal stability of SsoPox from the hyperthermophilic archaeon Sulfolobus solfataricus. (Articolo in rivista) (literal)

Anno

• 2009-01-01T00:00:00+01:00 (literal)

Alternative label

• Del Vecchio P, Elias M, Merone L, Graziano G, Dupuy J, Mandrich L, Carullo P, Fournier B, Rochu D, Rossi M, Masson P, Chabriere E, Manco G. (2009)
  Structural determinants of the high thermal stability of SsoPox from the hyperthermophilic archaeon Sulfolobus solfataricus.
  in Extremophiles (Tokyo, Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Del Vecchio P, Elias M, Merone L, Graziano G, Dupuy J, Mandrich L, Carullo P, Fournier B, Rochu D, Rossi M, Masson P, Chabriere E, Manco G. (literal)

Pagina inizio

• 461 (literal)

Pagina fine

• 470 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 13 (literal)

Rivista

• Extremophiles (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Titolo

• Structural determinants of the high thermal stability of SsoPox from the hyperthermophilic archaeon Sulfolobus solfataricus. (literal)

Abstract

• Organophosphates (OPs) constitute the largest class of insecticides used worldwide and certain of them are potent nerve agents. Consequently, enzymes degrading OPs are of paramount interest, as they could be used as bioscavengers and biodecontaminants. Looking for a stable OPs catalyst, able to support industrial process constraints, a hyperthermophilic phosphotriesterase (PTE) (SsoPox) was isolated from the archaeon Sulfolobus solfataricus and was found to be highly thermostable. The solved 3D structure revealed that SsoPox is a noncovalent dimer, with lactonase activity against \"quorum sensing signals\", and therefore could represent also a potential weapon against certain pathogens. The structural basis of the high thermostability of SsoPox has been investigated by performing a careful comparison between its structure and that of two mesophilic PTEs from Pseudomonas diminuta and Agrobacterium radiobacter. In addition, the conformational stability of SsoPox against the denaturing action of temperature and GuHCl has been determined by means of circular dichroism and fluorescence measurements. The data suggest that the two fundamental differences between SsoPox and the mesophilic counterparts are: (a) a larger number of surface salt bridges, also involved in complex networks; (b) a tighter quaternary structure due to an optimization of the interactions at the interface between the two monomers. (literal)

Prodotto di

• Institute of protein biochemistry (IBP) (Istituto)
• DR.RAIA: Basi molecolari dell'adattamento di cellule e proteine alle condizioni estreme: aspetti applicativi (SV.P17.001.001) (Modulo)
• DR. MANCO : Studi di idrolasi da fonti diverse e proteine vegetali. (SV.P14.010.001) (Modulo)

Autore CNR

• LUIGIA MERONE (Unità di personale esterno)
• LUIGI MANDRICH (Unità di personale interno)
• GIUSEPPE MANCO (Unità di personale interno)
• Mosè Rossi (Unità di personale esterno)

Incoming links:

Autore CNR di

• GIUSEPPE MANCO (Unità di personale interno)
• Mosè Rossi (Unità di personale esterno)
• LUIGIA MERONE (Unità di personale esterno)
• LUIGI MANDRICH (Unità di personale interno)

Prodotto

• Institute of protein biochemistry (IBP) (Istituto)
• DR. MANCO : Studi di idrolasi da fonti diverse e proteine vegetali. (SV.P14.010.001) (Modulo)
• DR.RAIA: Basi molecolari dell'adattamento di cellule e proteine alle condizioni estreme: aspetti applicativi (SV.P17.001.001) (Modulo)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Extremophiles (Rivista)