The structure of the SodCII-encoded monomeric Cu, Zn superoxide dismutase from Salmonella enterica has been solved by NMR spectroscopy. This represents the first solution structure of a natural and fully active monomeric superoxide dismutase in solution, providing information useful for the interpretation of the evolutional development of these enzymes. The protein scaffold consists of the characteristic beta-barrel common to the whole enzyme family. The general shape of the protein is quite similar to that of Escherichia coli Cu, Zn superoxide dismutase, although some differences are observed mainly in the active site. SodCII presents a more rigid conformation with respect to the engineered monomeric mutants of the human Cu, Zn superoxide dismutase, even though significant disorder is still present in the loops shaping the active site. The analysis of both dynamics and hydration properties of the protein in solution highlights the factors required to maintain the fully active and, at the same time, monomeric protein. This study provides novel insights into the functional differences between monomeric and dimeric bacterial Cu, Zn superoxide dismutases, in turn helping to explain the convergent evolution toward a dimeric structure in prokaryotic and eukaryotic enzymes of this class.

Mori, M., Jimenez, B., Piccioli, M., Battistoni, A., Sette, M. (2008). The solution structure of the monomeric copper, zinc superoxide dismutase from Salmonella enterica: structural insights to understand the evolution toward the dimeric structure. BIOCHEMISTRY, 47(49), 12954-12963 [10.1021/bi801252e].

The solution structure of the monomeric copper, zinc superoxide dismutase from Salmonella enterica: structural insights to understand the evolution toward the dimeric structure

Battistoni A;Sette M
2008-01-01

Abstract

The structure of the SodCII-encoded monomeric Cu, Zn superoxide dismutase from Salmonella enterica has been solved by NMR spectroscopy. This represents the first solution structure of a natural and fully active monomeric superoxide dismutase in solution, providing information useful for the interpretation of the evolutional development of these enzymes. The protein scaffold consists of the characteristic beta-barrel common to the whole enzyme family. The general shape of the protein is quite similar to that of Escherichia coli Cu, Zn superoxide dismutase, although some differences are observed mainly in the active site. SodCII presents a more rigid conformation with respect to the engineered monomeric mutants of the human Cu, Zn superoxide dismutase, even though significant disorder is still present in the loops shaping the active site. The analysis of both dynamics and hydration properties of the protein in solution highlights the factors required to maintain the fully active and, at the same time, monomeric protein. This study provides novel insights into the functional differences between monomeric and dimeric bacterial Cu, Zn superoxide dismutases, in turn helping to explain the convergent evolution toward a dimeric structure in prokaryotic and eukaryotic enzymes of this class.
2008
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/10 - BIOCHIMICA
English
Con Impact Factor ISI
Catalysts; Copper; Enzymes; Escherichia coli; Nuclear magnetic resonance; Nuclear magnetic resonance spectroscopy; Proteins; Zinc; Active sites; Convergent evolutions; Dimeric structures; Eukaryotic enzymes; Functional differences; Hydration properties; Nmr spectroscopies; Salmonella enterica; Solution structures; Structural insights; Superoxide dismutase; Superoxide dismutases; Oxygen; bacterial enzyme; copper zinc superoxide dismutase; article; carbon nuclear magnetic resonance; dimerization; enzyme active site; enzyme structure; Escherichia coli; human; metal binding; nitrogen nuclear magnetic resonance; nonhuman; polyacrylamide gel electrophoresis; priority journal; protein folding; proton nuclear magnetic resonance; Salmonella enterica; structure analysis; Bacteria (microorganisms); Escherichia coli; Eukaryota; Prokaryota; Salmonella enterica
Mori, M., Jimenez, B., Piccioli, M., Battistoni, A., Sette, M. (2008). The solution structure of the monomeric copper, zinc superoxide dismutase from Salmonella enterica: structural insights to understand the evolution toward the dimeric structure. BIOCHEMISTRY, 47(49), 12954-12963 [10.1021/bi801252e].
Mori, M; Jimenez, B; Piccioli, M; Battistoni, A; Sette, M
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/33760
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