3gl2

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[[Image:3gl2.png|left|200px]]
 
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{{STRUCTURE_3gl2| PDB=3gl2 | SCENE= }}
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==Crystal structure of dicamba monooxygenase bound to dicamba==
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<StructureSection load='3gl2' size='340' side='right'caption='[[3gl2]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3gl2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Stenotrophomonas_maltophilia Stenotrophomonas maltophilia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GL2 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]] 2.1&#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=D3M:3,6-DICHLORO-2-METHOXYBENZOIC+ACID'>D3M</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=3gl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gl2 OCA], [https://pdbe.org/3gl2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gl2 RCSB], [https://www.ebi.ac.uk/pdbsum/3gl2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gl2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DDMC_STEMA DDMC_STEMA] Component of the dicamba O-demethylase multicomponent enzyme system involved in the degradation of the herbicide dicamba (PubMed:15855162, PubMed:15820213, PubMed:16535584). In vitro, catalyzes the O-demethylation of 2-methoxy-3,6-dichlorobenzoic acid (dicamba) to yield 3,6-dichlorosalicylic acid (DCSA) via an exocyclic monooxygenation (PubMed:15855162, PubMed:15820213, PubMed:16535584, PubMed:19616009).<ref>PMID:15820213</ref> <ref>PMID:15855162</ref> <ref>PMID:16535584</ref> <ref>PMID:19616009</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/gl/3gl2_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=3gl2 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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Dicamba (3,6-dichloro-2-methoxybenzoic acid) is a widely used herbicide that is efficiently degraded by soil microbes. These microbes use a novel Rieske nonheme oxygenase, dicamba monooxygenase (DMO), to catalyze the oxidative demethylation of dicamba to 3,6-dichlorosalicylic acid (DCSA) and formaldehyde. We have determined the crystal structures of DMO in the free state, bound to its substrate dicamba, and bound to the product DCSA at 2.10-1.75 A resolution. The structures show that the DMO active site uses a combination of extensive hydrogen bonding and steric interactions to correctly orient chlorinated, ortho-substituted benzoic-acid-like substrates for catalysis. Unlike other Rieske aromatic oxygenases, DMO oxygenates the exocyclic methyl group, rather than the aromatic ring, of its substrate. This first crystal structure of a Rieske demethylase shows that the Rieske oxygenase structural scaffold can be co-opted to perform varied types of reactions on xenobiotic substrates.
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===Crystal structure of dicamba monooxygenase bound to dicamba===
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Crystal structure of dicamba monooxygenase: a Rieske nonheme oxygenase that catalyzes oxidative demethylation.,Dumitru R, Jiang WZ, Weeks DP, Wilson MA J Mol Biol. 2009 Sep 18;392(2):498-510. Epub 2009 Jul 15. PMID:19616011<ref>PMID:19616011</ref>
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{{ABSTRACT_PUBMED_19616011}}
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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 3gl2" style="background-color:#fffaf0;"></div>
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[[3gl2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Stenotrophomonas_maltophilia Stenotrophomonas maltophilia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GL2 OCA].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:019616011</ref><references group="xtra"/>
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Stenotrophomonas maltophilia]]
[[Category: Stenotrophomonas maltophilia]]
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[[Category: Dumitru, R.]]
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[[Category: Dumitru R]]
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[[Category: Jiang, W Z.]]
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[[Category: Jiang WZ]]
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[[Category: Weeks, D P.]]
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[[Category: Weeks DP]]
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[[Category: Wilson, M A.]]
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[[Category: Wilson MA]]
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[[Category: Non-heme mononuclear iron]]
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[[Category: Oxidoreductase]]
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[[Category: Oxygenase]]
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[[Category: Rieske protein]]
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Current revision

Crystal structure of dicamba monooxygenase bound to dicamba

PDB ID 3gl2

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