This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1eso
From Proteopedia
|
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 and 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 Sun Feb 3 09:39:27 2008
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
