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-{{STRUCTURE_4fav|  PDB=4fav  |  SCENE=  }}
-===Crystal Structure of WT MauG in Complex with Pre-Methylamine Dehydrogenase Aged 50 Days===
-{{ABSTRACT_PUBMED_23487750}}
-==Function==
+==Crystal Structure of WT MauG in Complex with Pre-Methylamine Dehydrogenase Aged 50 Days==
-[[http://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. [[http://www.uniprot.org/uniprot/DHML_PARDE DHML_PARDE]] Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin.
+<StructureSection load='4fav' size='340' side='right'caption='[[4fav]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4fav]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] and [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=4FAV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FAV FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.08&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0AF:7-HYDROXY-L-TRYPTOPHAN'>0AF</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fav OCA], [https://pdbe.org/4fav PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fav RCSB], [https://www.ebi.ac.uk/pdbsum/4fav PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fav ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Despite the importance of tryptophan (Trp) radicals in biology, very few radicals have been trapped and characterized in a physiologically meaningful context. Here we demonstrate that the diheme enzyme MauG uses Trp radical chemistry to catalyze formation of a Trp-derived tryptophan tryptophylquinone cofactor on its substrate protein, premethylamine dehydrogenase. The unusual six-electron oxidation that results in tryptophan tryptophylquinone formation occurs in three discrete two-electron catalytic steps. Here the exact order of these oxidation steps in the processive six-electron biosynthetic reaction is determined, and reaction intermediates are structurally characterized. The intermediates observed in crystal structures are also verified in solution using mass spectrometry. Furthermore, an unprecedented Trp-derived diradical species on premethylamine dehydrogenase, which is an intermediate in the first two-electron step, is characterized using high-frequency and -field electron paramagnetic resonance spectroscopy and UV-visible absorbance spectroscopy. This work defines a unique mechanism for radical-mediated catalysis of a protein substrate, and has broad implications in the areas of applied biocatalysis and understanding of oxidative protein modification during oxidative stress.
-==About this Structure==
+Diradical intermediate within the context of tryptophan tryptophylquinone biosynthesis.,Yukl ET, Liu F, Krzystek J, Shin S, Jensen LM, Davidson VL, Wilmot CM, Liu A Proc Natl Acad Sci U S A. 2013 Mar 19;110(12):4569-73. doi:, 10.1073/pnas.1215011110. Epub 2013 Mar 4. PMID:23487750<ref>PMID:23487750</ref>
-[[4fav]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans] and [http://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=4FAV OCA].
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4fav" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Methylamine dehydrogenase|Methylamine dehydrogenase]]
+*[[Methylamine utilisation protein|Methylamine utilisation protein]]
+*[[Methylation utilization protein MauG|Methylation utilization protein MauG]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Paracoccus denitrificans]]
-[[Category: Paracoccus denitrificans pd1222]]
+[[Category: Paracoccus denitrificans PD1222]]
-[[Category: Wilmot, C M.]]
+[[Category: Wilmot CM]]
-[[Category: Yukl, E T.]]
+[[Category: Yukl ET]]
-[[Category: Oxidoreductase-electron transfer complex]]
-[[Category: Oxidoreductase-electron transport complex]]
-[[Category: Tryptophan tryptophylquinone]]