1eso: Difference between revisions

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-[[Image:1eso.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1eso", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_1eso|  PDB=1eso  |  SCENE=  }}
-'''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]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
+<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>
+</table>
+== 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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/es/1eso_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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="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.
-==Overview==
+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>
-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==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-ESO 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].
+</div>
+<div class="pdbe-citations 1eso" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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]
+*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Superoxide dismutase]]
+[[Category: Battistoni A]]
-[[Category: Battistoni, A.]]
+[[Category: Bolognesi M]]
-[[Category: Bolognesi, M.]]
+[[Category: Capasso C]]
-[[Category: Capasso, C.]]
+[[Category: Desideri A]]
-[[Category: Desideri, A.]]
+[[Category: Folcarelli S]]
-[[Category: Folcarelli, S.]]
+[[Category: Pesce A]]
-[[Category: Pesce, A.]]
+[[Category: Rotilio G]]
-[[Category: Rotilio, G.]]
-[[Category: Copper enzyme]]
-[[Category: Cu,zn superoxide dismutase]]
-[[Category: Enzyme evolution]]
-[[Category: Monomeric superoxide dismutase]]
-[[Category: Oxidoreductase]]
-[[Category: X-ray crystal structure]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:28:27 2008''