1h1m

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(New page: 200px<br /> <applet load="1h1m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h1m, resolution 1.90&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1h1m.gif|left|200px]]<br />
 
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<applet load="1h1m" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1h1m, resolution 1.90&Aring;" />
 
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'''CRYSTAL STRUCTURE OF QUERCETIN 2,3-DIOXYGENASE ANAEROBICALLY COMPLEXED WITH THE SUBSTRATE KAEMPFEROL'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF QUERCETIN 2,3-DIOXYGENASE ANAEROBICALLY COMPLEXED WITH THE SUBSTRATE KAEMPFEROL==
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Quercetin 2,3-dioxygenase (2,3QD) is the only firmly established copper, dioxygenase known so far. Depending solely on a mononuclear Cu center, it, catalyzes the breakage of the O-heterocycle of flavonols, producing more, easily degradable phenolic carboxylic acid ester derivatives. In the, enzymatic process, two CC bonds are broken and concomitantly carbon, monoxide is released. The x-ray structures of Aspergillus japonicus 2,3QD, anaerobically complexed with the substrate kaempferol and the natural, substrate quercetin have been determined at 1.90- and 1.75-A resolution, respectively. Flavonols coordinate to the copper ion as monodentate, ligands through their 3OH group. They occupy a shallow and overall, hydrophobic cavity proximal to the metal center. As a result of a van der, Waals ... [[http://ispc.weizmann.ac.il/pmbin/getpm?12486225 (full description)]]
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<StructureSection load='1h1m' size='340' side='right'caption='[[1h1m]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1h1m]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_japonicus Aspergillus japonicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H1M 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]] 1.9&#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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=KMP:3,5,7-TRIHYDROXY-2-(4-HYDROXYPHENYL)-4H-CHROMEN-4-ONE'>KMP</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=1h1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h1m OCA], [https://pdbe.org/1h1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h1m RCSB], [https://www.ebi.ac.uk/pdbsum/1h1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h1m ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/QDOI_ASPJA QDOI_ASPJA] Performs the first step in the degradation of the flavonoid quercetin by a dioxygenase reaction. The enzyme catalyzes the cleavage of the O-heteroaromatic ring of the flavonol quercetin yielding the depside 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. This involves the remarkable dioxygenolytic cleavage of two carbon-carbon bonds.
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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/h1/1h1m_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=1h1m ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1H1M is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Aspergillus_japonicus Aspergillus japonicus]] with NAG, CU, KMP and MPD as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.24 1.13.11.24]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H1M OCA]].
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*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Anaerobic enzyme.substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase., Steiner RA, Kalk KH, Dijkstra BW, Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16625-30. Epub 2002 Dec 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12486225 12486225]
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[[Category: Aspergillus japonicus]]
[[Category: Aspergillus japonicus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Dijkstra, B.W.]]
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[[Category: Dijkstra BW]]
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[[Category: Steiner, R.A.]]
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[[Category: Steiner RA]]
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[[Category: CU]]
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[[Category: KMP]]
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[[Category: MPD]]
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[[Category: NAG]]
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[[Category: copper]]
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[[Category: dioxygenase]]
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[[Category: flavonol]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 17:23:05 2007''
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Current revision

CRYSTAL STRUCTURE OF QUERCETIN 2,3-DIOXYGENASE ANAEROBICALLY COMPLEXED WITH THE SUBSTRATE KAEMPFEROL

PDB ID 1h1m

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