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1eso
From Proteopedia
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|PDB= 1eso |SIZE=350|CAPTION= <scene name='initialview01'>1eso</scene>, resolution 2.0Å | |PDB= 1eso |SIZE=350|CAPTION= <scene name='initialview01'>1eso</scene>, resolution 2.0Å | ||
|SITE= <scene name='pdbsite=CUL:Cu+Ligands'>CUL</scene> and <scene name='pdbsite=ZNL:Zn+Ligands'>ZNL</scene> | |SITE= <scene name='pdbsite=CUL:Cu+Ligands'>CUL</scene> and <scene name='pdbsite=ZNL:Zn+Ligands'>ZNL</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span> |
|GENE= SODC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= SODC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eso OCA], [http://www.ebi.ac.uk/pdbsum/1eso PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eso RCSB]</span> | ||
}} | }} | ||
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[[Category: Pesce, A.]] | [[Category: Pesce, A.]] | ||
[[Category: Rotilio, G.]] | [[Category: Rotilio, G.]] | ||
| - | [[Category: CU]] | ||
| - | [[Category: ZN]] | ||
[[Category: copper enzyme]] | [[Category: copper enzyme]] | ||
| - | [[Category: cu]] | + | [[Category: cu,zn superoxide dismutase]] |
[[Category: enzyme evolution]] | [[Category: enzyme evolution]] | ||
[[Category: monomeric superoxide dismutase]] | [[Category: monomeric superoxide dismutase]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
[[Category: x-ray crystal structure]] | [[Category: x-ray crystal structure]] | ||
| - | [[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 Sun Mar 30 20:08:49 2008'' |
Revision as of 17:08, 30 March 2008
| |||||||
| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | , | ||||||
| Gene: | SODC (Escherichia coli) | ||||||
| Activity: | Superoxide dismutase, with EC number 1.15.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 20:08:49 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
