1r6y

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(New page: 200px<br /><applet load="1r6y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r6y, resolution 2.20&Aring;" /> '''Crystal structure of...)
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[[Image:1r6y.gif|left|200px]]<br /><applet load="1r6y" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1r6y, resolution 2.20&Aring;" />
 
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'''Crystal structure of YgiN from Escherichia coli'''<br />
 
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==Overview==
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==Crystal structure of YgiN from Escherichia coli==
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Naturally synthesized quinones perform a variety of important cellular, functions. Escherichia coli produce both ubiquinone and menaquinone, which, are involved in electron transport. However, semiquinone intermediates, produced during the one-electron reduction of these compounds, as well as, through auto-oxidation of the hydroxyquinone product, generate reactive, oxygen species that stress the cell. Here, we present the crystal, structure of YgiN, a protein of hitherto unknown function. The, three-dimensional fold of YgiN is similar to that of ActVA-Orf6, monooxygenase, which acts on hydroxyquinone substrates. YgiN shares a, promoter with "modulator of drug activity B," a protein with activity, similar to that of mammalian DT-diaphorase capable of reducing mendione., YgiN was able to reoxidize menadiol, the product of the "modulator of drug, activity B" (MdaB) enzymatic reaction. We therefore refer to YgiN as, quinol monooxygenase. Modulator of drug activity B is reported to be, involved in the protection of cells from reactive oxygen species formed, during single electron oxidation and reduction reactions. The enzymatic, activities, together with the structural characterization of YgiN, lend, evidence to the possible existence of a novel quinone redox cycle in E., coli.
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<StructureSection load='1r6y' size='340' side='right'caption='[[1r6y]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1r6y]] 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=1R6Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R6Y FirstGlance]. <br>
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1R6Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R6Y OCA].
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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]] 2.2&#8491;</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=1r6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r6y OCA], [https://pdbe.org/1r6y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r6y RCSB], [https://www.ebi.ac.uk/pdbsum/1r6y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r6y ProSAT], [https://www.topsan.org/Proteins/BSGI/1r6y TOPSAN]</span></td></tr>
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==Reference==
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</table>
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Structural and biochemical evidence for an enzymatic quinone redox cycle in Escherichia coli: identification of a novel quinol monooxygenase., Adams MA, Jia Z, J Biol Chem. 2005 Mar 4;280(9):8358-63. Epub 2004 Dec 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15613473 15613473]
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== Function ==
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[https://www.uniprot.org/uniprot/YGIN_ECOLI YGIN_ECOLI] Can oxidize menadiol to menadione.
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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/r6/1r6y_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=1r6y ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[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: Adams, M.A.]]
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[[Category: Adams MA]]
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[[Category: BSGI, Montreal-Kingston.Bacterial.Structural.Genomics.Initiative.]]
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[[Category: Jia Z]]
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[[Category: Jia, Z.]]
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[[Category: bsgi]]
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[[Category: ferredoxin-like fold]]
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[[Category: functional annotation]]
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[[Category: hypothetical protein]]
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[[Category: montreal-kingston bacterial structural genomics initiative]]
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[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:19:14 2007''
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Current revision

Crystal structure of YgiN from Escherichia coli

PDB ID 1r6y

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