1eso

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[[Image:1eso.gif|left|200px]]<br /><applet load="1eso" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1eso.gif|left|200px]]
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caption="1eso, resolution 2.0&Aring;" />
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'''MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI'''<br />
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{{Structure
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|PDB= 1eso |SIZE=350|CAPTION= <scene name='initialview01'>1eso</scene>, resolution 2.0&Aring;
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|SITE= <scene name='pdbsite=CUL:Cu+Ligands'>CUL</scene> and <scene name='pdbsite=ZNL:Zn+Ligands'>ZNL</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene>
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|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]
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|GENE= SODC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1ESO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Sites: <scene name='pdbsite=CUL:Cu+Ligands'>CUL</scene> and <scene name='pdbsite=ZNL:Zn+Ligands'>ZNL</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ESO OCA].
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1ESO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ESO OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9405149 9405149]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9405149 9405149]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: CU]]
[[Category: CU]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: copper enzymes]]
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[[Category: copper enzyme]]
[[Category: cu]]
[[Category: cu]]
[[Category: enzyme evolution]]
[[Category: enzyme evolution]]
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[[Category: zn superoxide dismutase]]
[[Category: zn superoxide dismutase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:59:50 2008''

Revision as of 08:59, 20 March 2008

Image:1eso.gif


PDB ID 1eso

Drag the structure with the mouse to rotate
, resolution 2.0Å
Sites: and
Ligands: and
Gene: SODC (Escherichia coli)
Activity: Superoxide dismutase, with EC number 1.15.1.1
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

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