1eso
From Proteopedia
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[[Image:1eso.gif|left|200px]] | [[Image:1eso.gif|left|200px]] | ||
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'''MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI''' | '''MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI''' | ||
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[[Category: Pesce, A.]] | [[Category: Pesce, A.]] | ||
[[Category: Rotilio, G.]] | [[Category: Rotilio, G.]] | ||
| - | [[Category: | + | [[Category: Copper enzyme]] |
| - | [[Category: | + | [[Category: Cu,zn superoxide dismutase]] |
| - | [[Category: | + | [[Category: Enzyme evolution]] |
| - | [[Category: | + | [[Category: Monomeric superoxide dismutase]] |
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| - | [[Category: | + | [[Category: X-ray crystal structure]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:28:27 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:28, 2 May 2008
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. 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 Fri May 2 15:28:27 2008
Categories: Escherichia coli | Single protein | Superoxide dismutase | Battistoni, A. | Bolognesi, M. | Capasso, C. | Desideri, A. | Folcarelli, S. | Pesce, A. | Rotilio, G. | Copper enzyme | Cu,zn superoxide dismutase | Enzyme evolution | Monomeric superoxide dismutase | Oxidoreductase | X-ray crystal structure
