A novel member of the protein disulfide oxidoreductase family from Aeropyrum pernix K1: structure, function and electrostatics. (Articolo in rivista)

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  • A novel member of the protein disulfide oxidoreductase family from Aeropyrum pernix K1: structure, function and electrostatics. (Articolo in rivista) (literal)
Anno
  • 2006-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.jmb.2006.07.038 (literal)
Alternative label
  • D'Ambrosio Katia; Pedone Emilia; Langella Emma; De Simone Giuseppina; Rossi Mose; Pedone Carlo; Bartolucci Simonetta. (2006)
    A novel member of the protein disulfide oxidoreductase family from Aeropyrum pernix K1: structure, function and electrostatics.
    in Journal of Molecular Biology
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • D'Ambrosio Katia; Pedone Emilia; Langella Emma; De Simone Giuseppina; Rossi Mose; Pedone Carlo; Bartolucci Simonetta. (literal)
Pagina inizio
  • 743 (literal)
Pagina fine
  • 752 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 362 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#descrizioneSinteticaDelProdotto
  • Pubblicazione su rivista internazionale (literal)
Note
  • ISI Web of Science (WOS) (literal)
  • Scopu (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Biostrutture e Bioimmagini, C.N.R., Napoli, Italy Istituto di Biochimica delle Proteine, C.N.R., Napoli, Italy Dipartimento delle Scienze Biologiche, Università degli Studi di Napoli \"Federico II\", Napoli, Italy Dipartimento di Biologia Strutturale e Funzionale, Università degli Studi di Napoli \"Federico II\", Napoli, Italy (literal)
Titolo
  • A novel member of the protein disulfide oxidoreductase family from Aeropyrum pernix K1: structure, function and electrostatics. (literal)
Abstract
  • The formation of disulfide bonds between cysteine residues is a ratelimiting step in protein folding. To control this oxidative process, different organisms have developed different systems. In bacteria, disulfide bond formation is assisted by the Dsb protein family; in eukarya, disulfide bond formation and rearrangement are catalyzed by PDI. In thermophilic organisms, a potential key role in disulfide bond formation has recently been ascribed to a new cytosolic Protein Disulphide Oxidoreductase family whose members have a molecular mass of about 26 kDa and are characterized by two thioredoxin folds comprising a CXXC active site motif each. Here we report on the functional and structural characterization of ApPDO, a new member of this family, which was isolated from the archaeon Aeropyrum pernix K1. Functional studies have revealed that ApPDO can catalyze the reduction, oxidation and isomerization of disulfide bridges. Structural studies have shown that this protein has two CXXC active sites with fairly similar geometrical parameters typical of a stable conformation. Finally, a theoretical calculation of the cysteine pKa values has suggested that the two active sites have similar functional properties and each of them can impart activity to the enzyme. Our results are evidence of functional similarity between the members of the Protein Disulphide Oxidoreductase family and the eukaryotic enzyme PDI. However, as the different three-dimensional features of these two biological systems strongly suggest significantly different mechanisms of action, further experimental studies will be needed to make clear how different three-dimensional structures can result in systems with similar functional behavior. (literal)
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