1eso

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[[Image:1eso.gif|left|200px]]
 
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{{Structure
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==MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI==
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|PDB= 1eso |SIZE=350|CAPTION= <scene name='initialview01'>1eso</scene>, resolution 2.0&Aring;
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<StructureSection load='1eso' size='340' side='right'caption='[[1eso]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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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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== Structural highlights ==
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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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<table><tr><td colspan='2'>[[1eso]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ESO FirstGlance]. <br>
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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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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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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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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eso OCA], [https://pdbe.org/1eso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eso RCSB], [https://www.ebi.ac.uk/pdbsum/1eso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eso ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SODC_ECOLI SODC_ECOLI] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/es/1eso_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1eso ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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'''MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI'''
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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:9405149<ref>PMID:9405149</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1eso" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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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].
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__TOC__
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</StructureSection>
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==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://www.ncbi.nlm.nih.gov/pubmed/9405149 9405149]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Superoxide dismutase]]
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[[Category: Battistoni A]]
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[[Category: Battistoni, A.]]
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[[Category: Bolognesi M]]
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[[Category: Bolognesi, M.]]
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[[Category: Capasso C]]
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[[Category: Capasso, C.]]
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[[Category: Desideri A]]
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[[Category: Desideri, A.]]
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[[Category: Folcarelli S]]
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[[Category: Folcarelli, S.]]
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[[Category: Pesce A]]
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[[Category: Pesce, A.]]
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[[Category: Rotilio G]]
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[[Category: Rotilio, G.]]
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[[Category: CU]]
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[[Category: ZN]]
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[[Category: copper enzyme]]
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[[Category: cu]]
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[[Category: enzyme evolution]]
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[[Category: monomeric superoxide dismutase]]
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[[Category: oxidoreductase]]
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[[Category: x-ray crystal structure]]
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[[Category: zn superoxide dismutase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:59:50 2008''
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Current revision

MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI

PDB ID 1eso

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