1eso
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The first three-dimensional structure of a functional monomeric Cu, Zn | + | 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== | ==About this Structure== | ||
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[[Category: zn superoxide dismutase]] | [[Category: zn superoxide dismutase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:05 2008'' |
Revision as of 10:31, 21 February 2008
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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 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 Thu Feb 21 12:31:05 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
