Sulfolobus solfataricus thiol redox puzzle: Characterization of an atypical protein disulfide oxidoreductase (Articolo in rivista)

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  • Sulfolobus solfataricus thiol redox puzzle: Characterization of an atypical protein disulfide oxidoreductase (Articolo in rivista) (literal)
Anno
  • 2014-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1007/s00792-013-0607-8 (literal)
Alternative label
  • Limauro D.; De Simone G.; Pirone L.; Bartolucci S.; D'Ambrosio K.; Pedone E. (2014)
    Sulfolobus solfataricus thiol redox puzzle: Characterization of an atypical protein disulfide oxidoreductase
    in Extremophiles (Tokyo, Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Limauro D.; De Simone G.; Pirone L.; Bartolucci S.; D'Ambrosio K.; Pedone E. (literal)
Pagina inizio
  • 219 (literal)
Pagina fine
  • 228 (literal)
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  • http://www.scopus.com/inward/record.url?eid=2-s2.0-84896736748&partnerID=q2rCbXpz (literal)
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  • 18 (literal)
Rivista
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  • 2 (literal)
Note
  • Scopu (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Dipartimento di Biologia, Università degli Studi di Napoli Federico II, Complesso Universitario Monte S. Angelo, Via Cinthia, 80126 Naples, Italy; Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134 Naples, Italy; Istituto di Cristallografia, CNR, Via Giovanni Amendola 122/O, 70126 Bari, Italy (literal)
Titolo
  • Sulfolobus solfataricus thiol redox puzzle: Characterization of an atypical protein disulfide oxidoreductase (literal)
Abstract
  • Protein disulfide oxidoreductases (PDOs) are proteins involved in disulfide bond formation playing a crucial role in adaptation to extreme environment. This paper reports the functional and structural characterization of Sso1120, a PDO from the hyperthermophilic archaeon Sulfolobus solfataricus. The protein was expressed in Escherichia coli and purified to homogeneity. The functional characterization showed that the enzyme has reductase activity, as tested by insulin assay, but differently from the other PDOs, it does not present isomerase activity. In addition it is able to form a redox couple with the thioredoxin reductase that could be used in undiscovered pathways. The protein revealed a melting point of around 90 °C in CD spectroscopy-monitored thermal denaturation and high denaturant resistance. The X-ray crystallographic structure was solved at 1.80 Å resolution, showing differences with respect to other PDOs and an unexpected similarity with the N-terminal domain of the alkyl hydroperoxide reductase F component from Salmonella typhimurium. On the basis of the reported data and of bioinformatics and phylogenetic analyses, a possible involvement of this atypical PDO in a new antioxidant system of S. solfataricus has been proposed. © 2013 Springer Japan. (literal)
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