4fa4 - Revision history

OCA at 02:52, 21 November 2024

2024-11-21T02:52:25Z

← Older revision		Revision as of 02:52, 21 November 2024
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	== Function ==		== 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.		[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.

			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>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 4fa4" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 15:		Line 24:
	*[[Methylamine utilisation protein\|Methylamine utilisation protein]]		*[[Methylamine utilisation protein\|Methylamine utilisation protein]]
	*[[Methylation utilization protein MauG\|Methylation utilization protein MauG]]		*[[Methylation utilization protein MauG\|Methylation utilization protein MauG]]
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 15:19, 14 March 2024

2024-03-14T15:19:51Z

← Older revision		Revision as of 15:19, 14 March 2024
Line 10:		Line 10:
	== Function ==		== 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.		[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.

	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>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4fa4" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
Line 24:		Line 15:
	*[[Methylamine utilisation protein\|Methylamine utilisation protein]]		*[[Methylamine utilisation protein\|Methylamine utilisation protein]]
	*[[Methylation utilization protein MauG\|Methylation utilization protein MauG]]		*[[Methylation utilization protein MauG\|Methylation utilization protein MauG]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:22, 6 December 2023

2023-12-06T08:22:06Z

← Older revision		Revision as of 08:22, 6 December 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fa4]] 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=4FA4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FA4 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4fa4]] 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=4FA4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FA4 FirstGlance]. <br>
	</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=ACT:ACETATE+ION'>ACT</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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.14Å</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=ACT:ACETATE+ION'>ACT</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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4fa4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fa4 OCA], [https://pdbe.org/4fa4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fa4 RCSB], [https://www.ebi.ac.uk/pdbsum/4fa4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fa4 ProSAT]</span></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=4fa4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fa4 OCA], [https://pdbe.org/4fa4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fa4 RCSB], [https://www.ebi.ac.uk/pdbsum/4fa4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fa4 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 04:44, 7 October 2022

2022-10-07T04:44:21Z

← Older revision		Revision as of 04:44, 7 October 2022
Line 1:		Line 1:

	==Crystal Structure of WT MauG in Complex with Pre-Methylamine Dehydrogenase Aged 10 Days==		==Crystal Structure of WT MauG in Complex with Pre-Methylamine Dehydrogenase Aged 10 Days==
	<StructureSection load='4fa4' size='340' side='right' caption='[[4fa4]], [[Resolution\|resolution]] 2.14Å' scene=''>		<StructureSection load='4fa4' size='340' side='right'caption='[[4fa4]], [[Resolution\|resolution]] 2.14Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fa4]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Atcc_17741 Atcc 17741~~] and [~~http~~://en.wikipedia.org/wiki/~~Pardp Pardp~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FA4 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4FA4 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4fa4]] 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=4FA4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FA4 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene~~></td></tr>~~		</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=ACT:ACETATE+ION'>ACT</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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
	~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=0AF:7-HYDROXY-L-TRYPTOPHAN'>0AF</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=4fa4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fa4 OCA], [https://pdbe.org/4fa4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fa4 RCSB], [https://www.ebi.ac.uk/pdbsum/4fa4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fa4 ProSAT]</span></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3l4m\|3l4m]], [[4fa5\|4fa5]], [[4fa9\|4fa9]], [[4fan\|4fan]], [[4fav\|4fav]], [[4fb1\|4fb1]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mauG, Pden_4736 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=318586 PARDP]), mauA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 ATCC 17741]), Pden_4730 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=318586 PARDP])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylamine_dehydrogenase_(amicyanin) Methylamine dehydrogenase (amicyanin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.9.1 1.4.9.1] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4fa4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fa4 OCA], [~~http~~://pdbe.org/4fa4 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4fa4 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4fa4 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4fa4 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[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~~.		[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;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 21:
	==See Also==		==See Also==
	*[[Methylamine dehydrogenase\|Methylamine dehydrogenase]]		*[[Methylamine dehydrogenase\|Methylamine dehydrogenase]]
			*[[Methylamine utilisation protein\|Methylamine utilisation protein]]
	*[[Methylation utilization protein MauG\|Methylation utilization protein MauG]]		*[[Methylation utilization protein MauG\|Methylation utilization protein MauG]]
	== References ==		== References ==
Line 30:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Atcc 17741~~]]		[[Category: Large Structures]]
	[[Category: ~~Pardp~~]]		[[Category: Paracoccus denitrificans]]
	[[Category: ~~Wilmot, C M~~]]		[[Category: Paracoccus denitrificans PD1222]]
	[[Category: ~~Yukl, E T~~]]		[[Category: Wilmot CM]]
	[[Category: ~~Oxidoreductase-electron transfer complex]]~~		[[Category: Yukl ET]]
	~~[[Category: Oxidoreductase-electron transport complex]]~~
	~~[[Category: Tryptophan tryptophylquinone~~]]

OCA at 08:08, 5 August 2016

2016-08-05T08:08:57Z

← Older revision		Revision as of 08:08, 5 August 2016
Line 1:		Line 1:

	==Crystal Structure of WT MauG in Complex with Pre-Methylamine Dehydrogenase Aged 10 Days==		==Crystal Structure of WT MauG in Complex with Pre-Methylamine Dehydrogenase Aged 10 Days==
	<StructureSection load='4fa4' size='340' side='right' caption='[[4fa4]], [[Resolution\|resolution]] 2.14Å' scene=''>		<StructureSection load='4fa4' size='340' side='right' caption='[[4fa4]], [[Resolution\|resolution]] 2.14Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4fa4]] 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=4FA4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FA4 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4fa4]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_17741 Atcc 17741] and [http://en.wikipedia.org/wiki/Pardp Pardp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FA4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FA4 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=0AF:7-HYDROXY-L-TRYPTOPHAN'>0AF</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=0AF:7-HYDROXY-L-TRYPTOPHAN'>0AF</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3l4m\|3l4m]], [[4fa5\|4fa5]], [[4fa9\|4fa9]], [[4fan\|4fan]], [[4fav\|4fav]], [[4fb1\|4fb1]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3l4m\|3l4m]], [[4fa5\|4fa5]], [[4fa9\|4fa9]], [[4fan\|4fan]], [[4fav\|4fav]], [[4fb1\|4fb1]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mauG, Pden_4736 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=318586 ~~Paracoccus denitrificans PD1222~~]), mauA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 ~~Paracoccus denitrificans~~]), Pden_4730 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=318586 ~~Paracoccus denitrificans PD1222~~])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mauG, Pden_4736 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=318586 PARDP]), mauA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 ATCC 17741]), Pden_4730 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=318586 PARDP])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylamine_dehydrogenase_(amicyanin) Methylamine dehydrogenase (amicyanin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.9.1 1.4.9.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylamine_dehydrogenase_(amicyanin) Methylamine dehydrogenase (amicyanin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.9.1 1.4.9.1] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fa4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fa4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fa4 RCSB], [http://www.ebi.ac.uk/pdbsum/4fa4 PDBsum]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fa4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fa4 OCA], [http://pdbe.org/4fa4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fa4 RCSB], [http://www.ebi.ac.uk/pdbsum/4fa4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fa4 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 20:		Line 21:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 4fa4" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Methylamine dehydrogenase\|Methylamine dehydrogenase]]		*[[Methylamine dehydrogenase\|Methylamine dehydrogenase]]
			*[[Methylation utilization protein MauG\|Methylation utilization protein MauG]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Paracoccus denitrificans~~]]		[[Category: Atcc 17741]]
	[[Category: ~~Paracoccus denitrificans pd1222~~]]		[[Category: Pardp]]
	[[Category: Wilmot, C M]]		[[Category: Wilmot, C M]]
	[[Category: Yukl, E T]]		[[Category: Yukl, E T]]

OCA at 17:09, 25 December 2014

2014-12-25T17:09:06Z

← Older revision		Revision as of 17:09, 25 December 2014
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	~~{{STRUCTURE_4fa4\| PDB=4fa4 \| SCENE= }}~~		==Crystal Structure of WT MauG in Complex with Pre-Methylamine Dehydrogenase Aged 10 Days==
	===Crystal Structure of WT MauG in Complex with Pre-Methylamine Dehydrogenase Aged 10 Days===		<StructureSection load='4fa4' size='340' side='right' caption='[[4fa4]], [[Resolution\|resolution]] 2.14Å' scene=''>
	~~{{ABSTRACT_PUBMED_23487750}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[4fa4]] 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=4FA4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FA4 FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
			<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=0AF:7-HYDROXY-L-TRYPTOPHAN'>0AF</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3l4m\|3l4m]], [[4fa5\|4fa5]], [[4fa9\|4fa9]], [[4fan\|4fan]], [[4fav\|4fav]], [[4fb1\|4fb1]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">mauG, Pden_4736 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=318586 Paracoccus denitrificans PD1222]), mauA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 Paracoccus denitrificans]), Pden_4730 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=318586 Paracoccus denitrificans PD1222])</td></tr>
			<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylamine_dehydrogenase_(amicyanin) Methylamine dehydrogenase (amicyanin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.9.1 1.4.9.1] </span></td></tr>
			<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fa4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fa4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fa4 RCSB], [http://www.ebi.ac.uk/pdbsum/4fa4 PDBsum]</span></td></tr>
			</table>
			== Function ==
			[[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.
			<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.

	~~==Function==~~		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>
	~~[[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~~.
			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>

	==~~About this Structure~~==		==See Also==
	[[~~4fa4~~]] ~~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=4FA4 OCA].		*[[Methylamine dehydrogenase\|Methylamine dehydrogenase]]
			== References ==
			<references/>
			__TOC__
			</StructureSection>
	[[Category: Paracoccus denitrificans]]		[[Category: Paracoccus denitrificans]]
	[[Category: Paracoccus denitrificans pd1222]]		[[Category: Paracoccus denitrificans pd1222]]
	[[Category: Wilmot, C M.]]		[[Category: Wilmot, C M]]
	[[Category: Yukl, E T.]]		[[Category: Yukl, E T]]
	[[Category: Oxidoreductase-electron transfer complex]]		[[Category: Oxidoreductase-electron transfer complex]]
	[[Category: Oxidoreductase-electron transport complex]]		[[Category: Oxidoreductase-electron transport complex]]
	[[Category: Tryptophan tryptophylquinone]]		[[Category: Tryptophan tryptophylquinone]]

OCA at 07:47, 27 March 2013

2013-03-27T07:47:35Z

← Older revision		Revision as of 07:47, 27 March 2013
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	~~[[Image:4fa4.jpg\|left\|200px]]~~

	{{STRUCTURE_4fa4\| PDB=4fa4 \| SCENE= }}		{{STRUCTURE_4fa4\| PDB=4fa4 \| SCENE= }}

	===Crystal Structure of WT MauG in Complex with Pre-Methylamine Dehydrogenase Aged 10 Days===		===Crystal Structure of WT MauG in Complex with Pre-Methylamine Dehydrogenase Aged 10 Days===
			{{ABSTRACT_PUBMED_23487750}}

			==Function==
			[[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.

	==About this Structure==		==About this Structure==

OCA at 14:25, 6 March 2013

2013-03-06T14:25:45Z

← Older revision		Revision as of 14:25, 6 March 2013
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	~~'''Unreleased structure'''~~		[[Image:4fa4.jpg\|left\|200px]]

	~~The entry~~ 4fa4 ~~is ON HOLD~~ ~~until Paper Publication~~		{{STRUCTURE_4fa4\| PDB=4fa4 \| SCENE= }}

	~~Authors: Yukl, E.T., Wilmot, C.M.~~		===Crystal Structure of WT MauG in Complex with Pre-Methylamine Dehydrogenase Aged 10 Days===

	~~Description: Crystal~~ Structure ~~of WT MauG in Complex~~ with ~~Pre~~-~~Methylamine Dehydrogenase Aged 10 Days~~
			==About this Structure==
			[[4fa4]] 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=4FA4 OCA].
			[[Category: Paracoccus denitrificans]]
			[[Category: Paracoccus denitrificans pd1222]]
			[[Category: Wilmot, C M.]]
			[[Category: Yukl, E T.]]
			[[Category: Oxidoreductase-electron transfer complex]]
			[[Category: Oxidoreductase-electron transport complex]]
			[[Category: Tryptophan tryptophylquinone]]

OCA at 05:27, 22 August 2012

2012-08-22T05:27:14Z

← Older revision		Revision as of 05:27, 22 August 2012
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4fa4 is ON HOLD		The entry 4fa4 is ON HOLD until Paper Publication

	Authors: Yukl, E.T., Wilmot, C.M.		Authors: Yukl, E.T., Wilmot, C.M.

	Description: Crystal Structure of WT MauG in Complex with Pre-Methylamine Dehydrogenase Aged 10 Days		Description: Crystal Structure of WT MauG in Complex with Pre-Methylamine Dehydrogenase Aged 10 Days

OCA: Protected "4fa4" [edit=sysop:move=sysop]

2012-05-30T05:33:30Z

Protected "4fa4" [edit=sysop:move=sysop]

← Older revision	Revision as of 05:33, 30 May 2012
(No difference)