1ESO

MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI

Summary for 1ESO

• Entry DOI: 10.2210/pdb1eso/pdb
• Descriptor: CU, ZN SUPEROXIDE DISMUTASE, ZINC ION, COPPER (II) ION, ... (4 entities in total)
• Functional Keywords: oxidoreductase, cu, zn superoxide dismutase, monomeric superoxide dismutase, copper enzymes, enzyme evolution, x-ray crystal structure
• Biological source: Escherichia coli
• Cellular location: Periplasm: P53635
• Total number of polymer chains: 1
• Total formula weight: 15889.54

Authors

Pesce, A.,Capasso, C.,Battistoni, A.,Folcarelli, S.,Rotilio, G.,Desideri, A.,Bolognesi, M. (deposition date: 1997-06-27, release date: 1998-07-01, Last modification date: 2024-11-06)

Primary citation

Pesce, A.,Capasso, C.,Battistoni, A.,Folcarelli, S.,Rotilio, G.,Desideri, A.,Bolognesi, M.
Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography.
J.Mol.Biol., 274:408-420, 1997

PubMed 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.

PubMed: 9405149
DOI: 10.1006/jmbi.1997.1400

Experimental method

X-RAY DIFFRACTION (2 Å)