Sulfolobus solfataricus protein disulphide oxidoreductase: insight into the roles of its redox sites (Articolo in rivista)

Type

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

Label

• Sulfolobus solfataricus protein disulphide oxidoreductase: insight into the roles of its redox sites (Articolo in rivista) (literal)

Anno

• 2009-01-01T00:00:00+01:00 (literal)

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

• 10.1093/protein/gzn061 (literal)

Alternative label

• Limauro, Danila; Saviano, Michele; Galdi, Ilaria; Rossi, Mose; Bartolucci, Simonetta; Pedone, Emilia (2009)
  Sulfolobus solfataricus protein disulphide oxidoreductase: insight into the roles of its redox sites
  in Protein engineering, design & selection (Online)
  (literal)

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

• Limauro, Danila; Saviano, Michele; Galdi, Ilaria; Rossi, Mose; Bartolucci, Simonetta; Pedone, Emilia (literal)

Pagina inizio

• 19 (literal)

Pagina fine

• 26 (literal)

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

• 22 (literal)

Rivista

• Protein engineering, design & selection (Rivista)

Note

• Scopu (literal)
• ISI Web of Science (WOS) (literal)

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

• 1Dip. Biologia Strutturale e Funzionale, University of Naples \"Federico II\", Complesso Universitario Monte S. Angelo, via Cinthia, 80126 Naples and 2Istituto di Biostrutture e Bioimmagini, C.N.R., Via Mezzocannone 16, 80134 Naples, Italy (literal)

Titolo

• Sulfolobus solfataricus protein disulphide oxidoreductase: insight into the roles of its redox sites (literal)

Abstract

• Sulfolobus solfataricus protein disulphide oxidoreductase (SsPDO) contains three disulphide bridges linking residues C41XXC44, C155XXC158, C173XXXXC178. To get information on the role played by these cross-links in determining the structural and functional properties of the protein, we performed site-directed mutagenesis on Cys residues and investigated the changes in folding, stability and functional features of the mutants and analysed the results with computational analysis. The reductase activity of SsPDO and its mutants was evaluated by insulin and thioredoxin reductase assays also coupled with peroxiredoxin Bcp1 of S. solfataricus. The threedimensional model of SsPDO was constructed and correlated with circular dichroism data and functional results. Biochemical analysis indicated a key function for the redox site constituted by Cys155 and Cys158. To discriminate between the role of the two cysteine residues, each cysteine was mutagenised and the behaviour of the single mutants was investigated elucidating the basis of the electron- shuffling mechanism for SsPDO. Finally, cysteine pK values were calculated and the accessible surface for the cysteine side chains in the reduced form was measured, showing higher reactivity and solvent exposure for Cys155. (literal)

Prodotto di

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Targeting e inibizione dell'angiogenesi per mezzo di antagonisti del recettore Flt-1 di VEGF/PlGF (PM.P01.007.001) (Modulo)

Autore CNR

• MICHELE SAVIANO (Persona)
• EMILIA MARIA PEDONE (Unità di personale interno)

Incoming links:

Autore CNR di

• MICHELE SAVIANO (Persona)
• EMILIA MARIA PEDONE (Unità di personale interno)

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Targeting e inibizione dell'angiogenesi per mezzo di antagonisti del recettore Flt-1 di VEGF/PlGF (PM.P01.007.001) (Modulo)

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

• Protein engineering, design & selection (Rivista)