PMID:9405149
| Citation |
Pesce, A, Capasso, C, Battistoni, A, Folcarelli, S, Rotilio, G, Desideri, A and Bolognesi, M (1997) Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography. J. Mol. Biol. 274:408-20 |
|---|---|
| Abstract |
The first three-dimensional structure of a functional monomeric Cu, Zn superoxide dismutase (from Escherichia coli, E_SOD) is reported at 2.0 A resolution (R-factor=16.8%). Compared to the homologous eukaryotic enzymes, E_SOD displays a perturbed antiparallel beta-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. |
| Links |
PubMed Online version:10.1006/jmbi.1997.1400 |
| Keywords |
Amino Acid Sequence; Binding Sites; Crystallography, X-Ray; Escherichia coli/enzymology; Models, Molecular; Molecular Sequence Data; Protein Conformation; Sequence Homology, Amino Acid; Superoxide Dismutase/chemistry; Superoxide Dismutase/metabolism |
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