3l4o

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[[Image:3l4o.png|left|200px]]
 
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{{STRUCTURE_3l4o| PDB=3l4o | SCENE= }}
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==Crystal Structure of the MauG/pre-Methylamine Dehydrogenase Complex After Treatment with Hydrogen Peroxide==
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<StructureSection load='3l4o' size='340' side='right'caption='[[3l4o]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3l4o]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans_PD1222 Paracoccus denitrificans PD1222]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L4O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L4O 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]] 2.046&#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=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</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=3l4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l4o OCA], [https://pdbe.org/3l4o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l4o RCSB], [https://www.ebi.ac.uk/pdbsum/3l4o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l4o ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MAUG_PARDP MAUG_PARDP] Involved in methylamine metabolism. Essential for the maturation of the beta subunit of MADH, presumably via a step in the biosynthesis of tryptophan tryptophylquinone (TTQ), the cofactor of MADH.
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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/l4/3l4o_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=3l4o 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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MauG is a diheme enzyme responsible for the posttranslational modification of two tryptophan residues to form the tryptophan tryptophylquinone (TTQ) cofactor of methylamine dehydrogenase (MADH). MauG converts preMADH, containing monohydroxylated betaTrp57, to fully functional MADH by catalyzing the insertion of a second oxygen atom into the indole ring and covalently linking betaTrp57 to betaTrp108. We have solved the x-ray crystal structure of MauG complexed with preMADH to 2.1 angstroms. The c-type heme irons and the nascent TTQ site are separated by long distances over which electron transfer must occur to achieve catalysis. In addition, one of the hemes has an atypical His-Tyr axial ligation. The crystalline protein complex is catalytically competent; upon addition of hydrogen peroxide, MauG-dependent TTQ synthesis occurs.
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===Crystal Structure of the MauG/pre-Methylamine Dehydrogenase Complex After Treatment with Hydrogen Peroxide===
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In crystallo posttranslational modification within a MauG/pre-methylamine dehydrogenase complex.,Jensen LM, Sanishvili R, Davidson VL, Wilmot CM Science. 2010 Mar 12;327(5971):1392-4. PMID:20223990<ref>PMID:20223990</ref>
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{{ABSTRACT_PUBMED_20223990}}
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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 3l4o" style="background-color:#fffaf0;"></div>
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[[3l4o]] is a 6 chain structure of [[Methylamine dehydrogenase]] with sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L4O OCA].
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==See Also==
==See Also==
*[[Methylamine dehydrogenase|Methylamine dehydrogenase]]
*[[Methylamine dehydrogenase|Methylamine dehydrogenase]]
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*[[Methylation utilization protein MauG|Methylation utilization protein MauG]]
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==Reference==
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== References ==
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<ref group="xtra">PMID:020223990</ref><references group="xtra"/>
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<references/>
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[[Category: Amine dehydrogenase]]
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__TOC__
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[[Category: Paracoccus denitrificans]]
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</StructureSection>
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[[Category: Jensen, L M.R.]]
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[[Category: Large Structures]]
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[[Category: Wilmot, C M.]]
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[[Category: Paracoccus denitrificans PD1222]]
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[[Category: C-heme]]
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[[Category: Jensen LMR]]
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[[Category: Disulfide bond]]
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[[Category: Wilmot CM]]
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[[Category: Electron transport]]
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[[Category: His-tyr heme]]
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[[Category: Iron]]
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[[Category: Maug]]
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[[Category: Metal-binding]]
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[[Category: Methylamine dehydrogenase]]
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[[Category: Oxidoreductase]]
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[[Category: Oxidoreductase-electron transport complex]]
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[[Category: Quinone cofactor]]
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[[Category: Transport]]
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[[Category: Ttq]]
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Current revision

Crystal Structure of the MauG/pre-Methylamine Dehydrogenase Complex After Treatment with Hydrogen Peroxide

PDB ID 3l4o

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