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1eso
From Proteopedia
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MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI
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, 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.
About this Structure
1ESO is a Single protein structure of sequence from Escherichia coli with ZN and CU as ligands. Active as Superoxide dismutase, with EC number 1.15.1.1 Known structural/functional Sites: and . 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
Page seeded by OCA on Tue Dec 18 15:13:39 2007
Categories: Escherichia coli | Single protein | Superoxide dismutase | Battistoni, A. | Bolognesi, M. | Capasso, C. | Desideri, A. | Folcarelli, S. | Pesce, A. | Rotilio, G. | CU | ZN | Copper enzymes | Cu | Enzyme evolution | Monomeric superoxide dismutase | Oxidoreductase | X-ray crystal structure | Zn superoxide dismutase
