The first three-dimensional structure of a functional monomeric Cu,Zn superoxide dismutase (from Escherichin coli, E_SOD) is reported at 2.0 Angstrom resolution (R-factor = 16.8%). Compared to the homologous eukaryotic enzymes, E SOD displays a perturbed antiparallel P-barrel structure. The most striking structural features observed include extended amino acid Insertions in the surface 1,2-loop and S-S subloop, modification of the disulfide bridge connection, and loss of functional electrostatic residues, suggesting a modified control of substrate steering toward the catalytic center. The active site Cu2+ displays a distorted coordination sphere due to an unusually long bond to the metal-bridging residue His61. Inspection of the crystal packing does not show regions of extended contact indicative of a dimeric assembly. The molecular surface region involved in subunit dimerization in eukaryotic superoxide dismutases is structurally altered in E_SOD and displays a net polar nature. (C) 1997 Academic Press Limited.

Pesce, A., Capasso, C., Battistoni, A., Folcarelli, S., Rotilio, G., Desideri, A., et al. (1997). Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography. JOURNAL OF MOLECULAR BIOLOGY, 274(3), 408-420 [10.1006/jmbi.1997.1400].

Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography

Battistoni A;Rotilio G;Desideri A;
1997-01-01

Abstract

The first three-dimensional structure of a functional monomeric Cu,Zn superoxide dismutase (from Escherichin coli, E_SOD) is reported at 2.0 Angstrom resolution (R-factor = 16.8%). Compared to the homologous eukaryotic enzymes, E SOD displays a perturbed antiparallel P-barrel structure. The most striking structural features observed include extended amino acid Insertions in the surface 1,2-loop and S-S subloop, modification of the disulfide bridge connection, and loss of functional electrostatic residues, suggesting a modified control of substrate steering toward the catalytic center. The active site Cu2+ displays a distorted coordination sphere due to an unusually long bond to the metal-bridging residue His61. Inspection of the crystal packing does not show regions of extended contact indicative of a dimeric assembly. The molecular surface region involved in subunit dimerization in eukaryotic superoxide dismutases is structurally altered in E_SOD and displays a net polar nature. (C) 1997 Academic Press Limited.
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Rilevanza internazionale
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Sì, ma tipo non specificato
Settore BIO/10
English
Con Impact Factor ISI
Cu,Zn superoxide dismutase; monomeric superoxide dismutase; copper enzymes; enzyme evolution; X-ray crystal structure
Pesce, A., Capasso, C., Battistoni, A., Folcarelli, S., Rotilio, G., Desideri, A., et al. (1997). Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography. JOURNAL OF MOLECULAR BIOLOGY, 274(3), 408-420 [10.1006/jmbi.1997.1400].
Pesce, A; Capasso, C; Battistoni, A; Folcarelli, S; Rotilio, G; Desideri, A; Bolognesi, M
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/55147
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