2ji1

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[[Image:2ji1.png|left|200px]]
 
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{{STRUCTURE_2ji1| PDB=2ji1 | SCENE= }}
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==X-ray structure of wild-type superoxide reductase from Desulfoarculus baarsii==
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<StructureSection load='2ji1' size='340' side='right'caption='[[2ji1]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<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>
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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]] 1.7&#8491;</td></tr>
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<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>
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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=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>
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</table>
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== Function ==
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[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>
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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/ji/2ji1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2ji1 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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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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===X-RAY STRUCTURE OF WILD-TYPE SUPEROXIDE REDUCTASE FROM DESULFOARCULUS BAARSII===
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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>
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{{ABSTRACT_PUBMED_17446401}}
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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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==About this Structure==
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<div class="pdbe-citations 2ji1" style="background-color:#fffaf0;"></div>
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[[2ji1]] is a 4 chain structure with sequence from [http://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].
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==See Also==
==See Also==
*[[Superoxide Reductase|Superoxide Reductase]]
*[[Superoxide Reductase|Superoxide Reductase]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:017446401</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Desulfarculus baarsii]]
[[Category: Desulfarculus baarsii]]
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[[Category: Superoxide reductase]]
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[[Category: Large Structures]]
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[[Category: Adam, V.]]
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[[Category: Adam V]]
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[[Category: Amara, P.]]
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[[Category: Amara P]]
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[[Category: Bourgeois, D.]]
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[[Category: Bourgeois D]]
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[[Category: Carpentier, P.]]
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[[Category: Carpentier P]]
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[[Category: Katona, G.]]
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[[Category: Katona G]]
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[[Category: Niviere, V.]]
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[[Category: Niviere V]]
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[[Category: Ohana, J.]]
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[[Category: Ohana J]]
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[[Category: Tsanov, N.]]
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[[Category: Tsanov N]]
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[[Category: Detoxification]]
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[[Category: Electron transport]]
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[[Category: Intermediate trapping]]
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[[Category: Iron]]
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[[Category: Metal-binding]]
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[[Category: Microspectrophotometry]]
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[[Category: Oxidoreductase]]
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[[Category: Raman spectroscopy]]
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[[Category: Redox state]]
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[[Category: Superoxide reductase]]
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[[Category: Transport]]
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Current revision

X-ray structure of wild-type superoxide reductase from Desulfoarculus baarsii

PDB ID 2ji1

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