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

@article{Pesce1997UniqueSF,
  title={Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography.},
  author={Alessandra Pesce and Clemente Capasso and Andrea Battistoni and S Folcarelli and Giuseppe Rotilio and Alessandro Desideri and Martino Bolognesi},
  journal={Journal of molecular biology},
  year={1997},
  volume={274 3},
  pages={408-20}
}
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… CONTINUE READING
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