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1eso
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==MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI== | ==MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI== | ||
| - | <StructureSection load='1eso' size='340' side='right' caption='[[1eso]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='1eso' size='340' side='right'caption='[[1eso]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1eso]] is a 1 chain structure with sequence from [ | + | <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> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id=' | + | <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> |
| - | + | <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> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [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. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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]. | </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]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
| - | + | ==See Also== | |
| - | + | *[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Battistoni | + | [[Category: Battistoni A]] |
| - | [[Category: Bolognesi | + | [[Category: Bolognesi M]] |
| - | [[Category: Capasso | + | [[Category: Capasso C]] |
| - | [[Category: Desideri | + | [[Category: Desideri A]] |
| - | [[Category: Folcarelli | + | [[Category: Folcarelli S]] |
| - | [[Category: Pesce | + | [[Category: Pesce A]] |
| - | [[Category: Rotilio | + | [[Category: Rotilio G]] |
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Current revision
MONOMERIC CU,ZN SUPEROXIDE DISMUTASE FROM ESCHERICHIA COLI
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