Insights on a new PDI-like family: structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus. (Articolo in rivista)

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Label
  • Insights on a new PDI-like family: structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus. (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.2005.11.041 (literal)
Alternative label
  • Pedone E., D’Ambrosio K., De Simone G., Rossi M., Pedone C., Bartolucci S. (2006)
    Insights on a new PDI-like family: structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus.
    in Journal of Molecular Biology
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Pedone E., D’Ambrosio K., De Simone G., Rossi M., Pedone C., Bartolucci S. (literal)
Pagina inizio
  • 155 (literal)
Pagina fine
  • 164 (literal)
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  • 356 (literal)
Rivista
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  • Pubblicazione su rivista scientifica internazionale (literal)
Note
  • ISI Web of Science (WOS) (literal)
  • Scopu (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1Istituto di Biostrutture e Bioimmagini, C.N.R., Napoli Italy 2Istituto di Biochimica delle Proteine, C.N.R., Napoli, Italy 3Dipartimento delle Scienze Biologiche, Universita` degli Studi di Napoli \"Federico II\" Napoli, Italy 4Dipartimento di Biologia Strutturale e Funzionale Universita` degli Studi di Napoli \"Federico II\", Napoli, Italy (literal)
Titolo
  • Insights on a new PDI-like family: structural and functional analysis of a protein disulfide oxidoreductase from the bacterium Aquifex aeolicus. (literal)
Abstract
  • A potential role in disulfide bond formation in the intracellular proteins of thermophilic organisms has recently been attributed to a new family of protein disulfide isomerase (PDI)-like proteins. Members of this family are characterized by a molecular mass of about 26 kDa and by two Trx folds, each comprising a CXXC active site motif. We report on the functional and structural characterization of a new member of this family, which was isolated from the thermophilic bacterium Aquifex aeolicus (AaPDO). Functional studies have revealed the high catalytic efficiency of this enzyme in reducing, oxidizing and isomerizing disulfide bridges. Site-directed mutagenesis experiments have suggested that its two active sites have similar functional properties, i.e. that each of them imparts partial activity to the enzyme. This similarity was confirmed by the analysis of the enzyme crystal structure, which points to similar geometrical parameters and solvent accessibilities for the two active sites. The results demonstrated that AaPDO is the most PDI-like of all prokaryotic proteins so far known. Thus, further experimental studies on this enzyme are likely to provide important information on the eukaryotic homologue. (literal)
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