1eso

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[[Image:1eso.gif|left|200px]]
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{{STRUCTURE_1eso| PDB=1eso | SCENE= }}
{{STRUCTURE_1eso| PDB=1eso | SCENE= }}
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'''MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI'''
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===MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9405149 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9405149}}
==About this Structure==
==About this Structure==
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[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: X-ray crystal structure]]
[[Category: X-ray crystal structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 01:50:33 2008''

Revision as of 22:50, 30 June 2008

Template:STRUCTURE 1eso

MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI

Template:ABSTRACT PUBMED 9405149

About this Structure

1ESO is a Single protein structure of sequence from Escherichia coli. 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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