Structural and functional insights into Aeropyrum pernix OppA, a member of a novel archaeal OppA subfamily. (Articolo in rivista)

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  • Structural and functional insights into Aeropyrum pernix OppA, a member of a novel archaeal OppA subfamily. (Articolo in rivista) (literal)
Anno
  • 2011-01-01T00:00:00+01:00 (literal)
Alternative label
  • Balestrieri M, Gogliettino M, Fiume I, Pocsfalvi G, Catara G, Rossi M, Palmieri G. (2011)
    Structural and functional insights into Aeropyrum pernix OppA, a member of a novel archaeal OppA subfamily.
    in Journal of bacteriology (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Balestrieri M, Gogliettino M, Fiume I, Pocsfalvi G, Catara G, Rossi M, Palmieri G. (literal)
Pagina inizio
  • 620 (literal)
Pagina fine
  • 630 (literal)
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  • 193 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#note
  • PubMed N. e link: PMID: 21097609 http://www.ncbi.nlm.nih.gov/pubmed/21097609 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Titolo
  • Structural and functional insights into Aeropyrum pernix OppA, a member of a novel archaeal OppA subfamily. (literal)
Abstract
  • In this study we gain insight into the structural and functional characterization of the oligopeptide-binding protein (OppAAp) previously identified from the extracellular media of Aeropyrum pernix cell culture at late stationary phase. OppAAp showed the N-terminus Q32 in a pyroglutamate form and a C-terminal processing at the level of a threonine rich region, probably involved in protein membrane anchoring. Moreover, the medium - released OppAAp was identified as a 'nicked' form composed of two fragments tightly associated, detachable only under strong denaturing conditions. The cleavage site E569-G570, seems be located on an exposed surface-loop, highly conserved in several 3D structures of di/oligopeptide binding proteins from different sources. Structural and biochemical properties of the 'nicked' protein were virtually indistinguishable from those of the intact form. Indeed studies on the entire bacterial-expressed OppAAp owning the same N- and C-terminus of the 'nicked' form, supported these findings. Moreover, in the middle exponential growth phase, OppAAp was found as intact cell membrane-associated protein. Interestingly, the native exoprotein OppAAp was co-purified with an hexapeptide (EKFKIV) showing both lysines methylated and possibly originated from an A. pernix endogenous stress-induced lipoprotein. Therefore, the involvement of OppAAp in recycling endogenous proteins, was suggested as potential physiological function. Finally, a new OppA from Sulfolobus solfataricus, SSO1288, was purified and preliminary characterized, allowing to identify a common structural/genetic organization shared by all the \"true\" archaeal OppAs of the di/oligopeptide class. (literal)
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