1eso | pdb_00001eso
MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI
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Overview
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, ... [(full description)]
About this Structure
1ESO is a [Single protein] structure of sequence from [Escherichia coli] with ZN and CU as [ligands]. Active as [[1]], with EC number [1.15.1.1]. Full crystallographic information is available from [OCA].
Reference
Unique structural features of the monomeric Cu,Zn superoxide dismutase from Escherichia coli, revealed by X-ray crystallography., Pesce A, Capasso C, Battistoni A, Folcarelli S, Rotilio G, Desideri A, Bolognesi M, J Mol Biol. 1997 Dec 5;274(3):408-20. PMID:9405149
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