The crystal structure of the superoxide dismutase from Helicobacter pylori reveals a structured C-terminal extension (Articolo in rivista)

Type
Label
  • The crystal structure of the superoxide dismutase from Helicobacter pylori reveals a structured C-terminal extension (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.bbapap.2008.04.024 (literal)
Alternative label
  • Esposito L.; Seydel A.; Aiello R.; Sorrentino G.; Cendron L.; Zanotti G.; Zagari A. (2008)
    The crystal structure of the superoxide dismutase from Helicobacter pylori reveals a structured C-terminal extension
    in Biochimica et biophysica acta. Proteins and proteomics
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Esposito L.; Seydel A.; Aiello R.; Sorrentino G.; Cendron L.; Zanotti G.; Zagari A. (literal)
Pagina inizio
  • 1601 (literal)
Pagina fine
  • 1606 (literal)
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  • 1784 (literal)
Rivista
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  • Pubblicazione su rivista internazionale (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, I-80134, Naples, Italy Department of Chemistry, University of Padua and Institute of Biomolecular Chemistry, CNR Padua Padua, Italy Venetian Institute of Molecular Medicine (VIMM), Padua, Italy Department of Biological Sciences and CNISM, University of Naples \" Federico II\", Naples, Italy CEINGE, Advanced Biotechnologies, Scarl, Naples, Italy (literal)
Titolo
  • The crystal structure of the superoxide dismutase from Helicobacter pylori reveals a structured C-terminal extension (literal)
Abstract
  • Superoxide dismutases (SODs) are key enzymes for fighting oxidative stress. Helicobacter pylori produces a single SOD (HpSOD) which contains iron. The structure of this antioxidant protein has been determined at 2.4 Å resolution. It is a dimer of two identical subunits with one iron ion per monomer. The protein shares 53% sequence identity with the corresponding enzyme from Escherichia coli. The model is compared with those of other dimeric Fe-containing SODs. HpSOD shows significant differences in relation to other SODs, the most important being an extended C-terminal tail. This structure provides a model for closely related sequences from species such as Campylobacter, where no structures are currently known. The structure of extended carboxyl termini is discussed in light of putative functions it may serve. (literal)
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