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2h90

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(New page: 200px<br /><applet load="2h90" size="350" color="white" frame="true" align="right" spinBox="true" caption="2h90, resolution 1.42&Aring;" /> '''Xenobiotic reductase...)
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[[Image:2h90.gif|left|200px]]<br /><applet load="2h90" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2h90, resolution 1.42&Aring;" />
 
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'''Xenobiotic reductase A in complex with coumarin'''<br />
 
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==Overview==
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==Xenobiotic reductase A in complex with coumarin==
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A continuous evolutionary pressure of the biotic and abiotic world has led, to the development of a diversity of microbial pathways to degrade and, biomineralize aromatic and heteroaromatic compounds. The heterogeneity of, compounds metabolized by bacteria like Pseudomonas putida indicates the, large variety of enzymes necessary to catalyse the required reactions., Quinoline, a N-heterocyclic aromatic compound, can be degraded by microbes, along different pathways. For P. putida 86 quinoline degradation by the, 8-hydroxycoumarin pathway has been described and several intermediates, were identified. To select enzymes catalysing the later stages of the, 8-hydroxycoumarin pathway P. putida 86 was grown with quinoline. The, FMN-containing enzyme xenobiotic reductase A (XenA) was isolated and, analysed for its reactivity with intermediates of the 8-hydroxycoumarin, pathway. XenA catalyses the NADPH-dependent reduction of 8-hydroxycoumarin, and coumarin to produce 8-hydroxy-3,4-dihydrocoumarin and, 3,4-dihydrocoumarin, respectively. Crystallographic analysis of XenA alone, and in complex with the two substrates revealed insights into the, mechanism. XenA shows a dimeric arrangement of two (beta/alpha)(8) barrel, domains each binding one FMN cofactor. High resolution crystal structures, of complexes with 8-hydroxycoumarin and coumarin show different modes of, binding for these molecules in the active site. While coumarin is ideally, positioned for hydride transfer from N-5 of the isoalloxazine ring to C-4, of coumarin, 8-hydroxycoumarin forms a non-productive complex with, oxidised XenA. Orientation of 8-hydroxycoumarin in the active site appears, to be dependent on the electronic state of the flavin. We postulate that, XenA catalyses the last step of the 8-hydroxycoumarin pathway before the, heterocyclic ring is hydrolysed to yield 3-(2,3-dihydroxyphenyl)-propionic, acid. As XenA is also found in P. putida strains unable to degrade, quinoline, it appears to have more than one physiological function and is, an example of how enzymes with low substrate specificity can help to, explain the variety of degradation pathways possible.
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<StructureSection load='2h90' size='340' side='right'caption='[[2h90]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[2h90]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H90 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H90 FirstGlance]. <br>
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2H90 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=FMN:'>FMN</scene>, <scene name='pdbligand=COU:'>COU</scene> and <scene name='pdbligand=BU3:'>BU3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H90 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]] 1.42&#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=BU3:(R,R)-2,3-BUTANEDIOL'>BU3</scene>, <scene name='pdbligand=COU:COUMARIN'>COU</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2h90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h90 OCA], [https://pdbe.org/2h90 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h90 RCSB], [https://www.ebi.ac.uk/pdbsum/2h90 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h90 ProSAT]</span></td></tr>
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Xenobiotic reductase A in the degradation of quinoline by Pseudomonas putida 86: physiological function, structure and mechanism of 8-hydroxycoumarin reduction., Griese JJ, P Jakob R, Schwarzinger S, Dobbek H, J Mol Biol. 2006 Aug 4;361(1):140-52. Epub 2006 Jun 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16822524 16822524]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q88NF7_PSEPK Q88NF7_PSEPK]
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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/h9/2h90_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=2h90 ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
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[[Category: Single protein]]
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[[Category: Dobbek H]]
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[[Category: Dobbek, H.]]
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[[Category: BU3]]
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[[Category: COU]]
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[[Category: FMN]]
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[[Category: SO4]]
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[[Category: beta-alpha-barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:16:40 2008''
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Current revision

Xenobiotic reductase A in complex with coumarin

PDB ID 2h90

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