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1tuv

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(New page: 200px<br /><applet load="1tuv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tuv, resolution 1.70&Aring;" /> '''Crystal structure of...)
Current revision (08:42, 14 February 2024) (edit) (undo)
 
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[[Image:1tuv.gif|left|200px]]<br /><applet load="1tuv" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1tuv, resolution 1.70&Aring;" />
 
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'''Crystal structure of YgiN in complex with menadione'''<br />
 
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==Overview==
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==Crystal structure of YgiN in complex with menadione==
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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='1tuv' size='340' side='right'caption='[[1tuv]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1tuv]] 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=1TUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TUV FirstGlance]. <br>
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1TUV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with VK3 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TUV 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]] 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=VK3:MENADIONE'>VK3</scene></td></tr>
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==Reference==
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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=1tuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tuv OCA], [https://pdbe.org/1tuv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tuv RCSB], [https://www.ebi.ac.uk/pdbsum/1tuv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tuv ProSAT]</span></td></tr>
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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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</table>
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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/tu/1tuv_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=1tuv 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: Jia, Z.]]
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[[Category: Jia Z]]
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[[Category: VK3]]
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[[Category: co-crystal with natural product]]
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[[Category: ferredoxin fold]]
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[[Category: menadione oxidase]]
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[[Category: monooxygenase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:36:38 2007''
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Current revision

Crystal structure of YgiN in complex with menadione

PDB ID 1tuv

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