2ji1
From Proteopedia
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| - | [[Image:2ji1.gif|left|200px]]<br /><applet load="2ji1" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2ji1, resolution 1.70Å" /> | ||
| - | '''X-RAY STRUCTURE OF WILD-TYPE SUPEROXIDE REDUCTASE FROM DESULFOARCULUS BAARSII'''<br /> | ||
| - | == | + | ==X-ray structure of wild-type superoxide reductase from Desulfoarculus baarsii== |
| - | + | <StructureSection load='2ji1' size='340' side='right'caption='[[2ji1]], [[Resolution|resolution]] 1.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2ji1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfarculus_baarsii Desulfarculus baarsii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JI1 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]] 1.7Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</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=2ji1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ji1 OCA], [https://pdbe.org/2ji1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ji1 RCSB], [https://www.ebi.ac.uk/pdbsum/2ji1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ji1 ProSAT]</span></td></tr> |
| - | + | </table> | |
| - | [ | + | == Function == |
| - | [ | + | [https://www.uniprot.org/uniprot/DFX_DESB2 DFX_DESB2] Catalyzes the one-electron reduction of superoxide anion radical to hydrogen peroxide at a nonheme ferrous iron center. Plays a fundamental role in case of oxidative stress via its superoxide detoxification activity.<ref>PMID:10617593</ref> |
| - | + | == 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/ji/2ji1_consurf.spt"</scriptWhenChecked> | |
| - | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2ji1 ConSurf]. | |
| - | [ | + | <div style="clear:both"></div> |
| - | [[ | + | <div style="background-color:#fffaf0;"> |
| - | [ | + | == Publication Abstract from PubMed == |
| - | + | Iron-peroxide intermediates are central in the reaction cycle of many iron-containing biomolecules. We trapped iron(III)-(hydro)peroxo species in crystals of superoxide reductase (SOR), a nonheme mononuclear iron enzyme that scavenges superoxide radicals. X-ray diffraction data at 1.95 angstrom resolution and Raman spectra recorded in crystallo revealed iron-(hydro)peroxo intermediates with the (hydro)peroxo group bound end-on. The dynamic SOR active site promotes the formation of transient hydrogen bond networks, which presumably assist the cleavage of the iron-oxygen bond in order to release the reaction product, hydrogen peroxide. | |
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| - | + | Raman-assisted crystallography reveals end-on peroxide intermediates in a nonheme iron enzyme.,Katona G, Carpentier P, Niviere V, Amara P, Adam V, Ohana J, Tsanov N, Bourgeois D Science. 2007 Apr 20;316(5823):449-53. PMID:17446401<ref>PMID:17446401</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2ji1" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Superoxide Reductase|Superoxide Reductase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Desulfarculus baarsii]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Adam V]] | ||
| + | [[Category: Amara P]] | ||
| + | [[Category: Bourgeois D]] | ||
| + | [[Category: Carpentier P]] | ||
| + | [[Category: Katona G]] | ||
| + | [[Category: Niviere V]] | ||
| + | [[Category: Ohana J]] | ||
| + | [[Category: Tsanov N]] | ||
Current revision
X-ray structure of wild-type superoxide reductase from Desulfoarculus baarsii
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Categories: Desulfarculus baarsii | Large Structures | Adam V | Amara P | Bourgeois D | Carpentier P | Katona G | Niviere V | Ohana J | Tsanov N
