7nkg - Revision history

OCA at 12:35, 1 February 2024

2024-02-01T12:35:50Z

←Older revision		Revision as of 12:35, 1 February 2024
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-	====	+	==Methyl-coenzyme M reductase from Methermicoccus shengliensis at 1.6-A resolution==
-	<StructureSection load='7nkg' size='340' side='right'caption='[[7nkg]]' scene=''>	+	<StructureSection load='7nkg' size='340' side='right'caption='[[7nkg]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7nkg]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Methermicoccus_shengliensis_DSM_18856 Methermicoccus shengliensis DSM 18856]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NKG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NKG FirstGlance]. <br>
-	</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=7nkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nkg OCA], [https://pdbe.org/7nkg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nkg RCSB], [https://www.ebi.ac.uk/pdbsum/7nkg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nkg ProSAT]</span></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]] 1.6Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGM:5-METHYL-ARGININE'>AGM</scene>, <scene name='pdbligand=COM:1-THIOETHANESULFONIC+ACID'>COM</scene>, <scene name='pdbligand=F43:FACTOR+430'>F43</scene>, <scene name='pdbligand=GL3:THIOGLYCIN'>GL3</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MHS:N1-METHYLATED+HISTIDINE'>MHS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TP7:COENZYME+B'>TP7</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=7nkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nkg OCA], [https://pdbe.org/7nkg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nkg RCSB], [https://www.ebi.ac.uk/pdbsum/7nkg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nkg ProSAT]</span></td></tr>
	</table>		</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Methanogenic archaea operate an ancient, if not primordial, metabolic pathway that releases methane as an end-product. This last step is orchestrated by the methyl-coenzyme M reductase (MCR), which uses a nickel-containing F(430)-cofactor as the catalyst. MCR astounds the scientific world by its unique reaction chemistry, its numerous post-translational modifications, and its importance in biotechnology not only for production but also for capturing the greenhouse gas methane. In this report, we investigated MCR natively isolated from Methermicoccus shengliensis. This methanogen was isolated from a high-temperature oil reservoir and has recently been shown to convert lignin and coal derivatives into methane through a process called methoxydotrophic methanogenesis. A methoxydotrophic culture was obtained by growing M. shengliensis with 3,4,5-trimethoxybenzoate as the main carbon and energy source. Under these conditions, MCR represents more than 12% of the total protein content. The native MCR structure refined at a resolution of 1.6-A precisely depicts the organization of a dimer of heterotrimers. Despite subtle surface remodeling and complete conservation of its active site with other homologues, MCR from the thermophile M. shengliensis contains the most limited number of post-translational modifications reported so far, questioning their physiological relevance in other relatives.
		+
		+	Structural Insights into the Methane-Generating Enzyme from a Methoxydotrophic Methanogen Reveal a Restrained Gallery of Post-Translational Modifications.,Kurth JM, Muller MC, Welte CU, Wagner T Microorganisms. 2021 Apr 14;9(4):837. doi: 10.3390/microorganisms9040837. PMID:33919946<ref>PMID:33919946</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7nkg" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Z-disk~~]]	+	[[Category: Methermicoccus shengliensis DSM 18856]]
		+	[[Category: Mueller M]]
		+	[[Category: Wagner T]]

OCA at 10:11, 19 May 2021

2021-05-19T10:11:23Z

←Older revision		Revision as of 10:11, 19 May 2021
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-	'''Unreleased structure'''

-	~~The entry~~ 7nkg ~~is ON HOLD until Paper Publication~~	+	====
-		+	<StructureSection load='7nkg' size='340' side='right'caption='[[7nkg]]' scene=''>
-	~~Authors~~: ~~Mueller, M~~.~~, Wagner, T~~.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
-	~~Description~~: ~~Methyl-coenzyme M reductase from Methermicoccus shengliensis at 1~~.6-~~A resolution~~	+	</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=7nkg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nkg OCA], [https://pdbe.org/7nkg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nkg RCSB], [https://www.ebi.ac.uk/pdbsum/7nkg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nkg ProSAT]</span></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	</table>
-	[[Category: ~~Wagner, T~~]]	+	__TOC__
-	[[Category: ~~Mueller, M~~]]	+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Z-disk]]

OCA at 13:32, 3 March 2021

2021-03-03T13:32:29Z

←Older revision		Revision as of 13:32, 3 March 2021
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 7nkg is ON HOLD	+	The entry 7nkg is ON HOLD until Paper Publication

	Authors: Mueller, M., Wagner, T.		Authors: Mueller, M., Wagner, T.

OCA: Protected "7nkg" [edit=sysop:move=sysop]

2021-02-24T05:48:33Z

Protected "7nkg" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:48, 24 February 2021

OCA: New page: '''Unreleased structure''' The entry 7nkg is ON HOLD Authors: Mueller, M., Wagner, T. Description: Methyl-coenzyme M reductase from Methermicoccus shengliensis at 1.6-A resolution [[Ca...

2021-02-24T05:48:32Z

New page: '''Unreleased structure''' The entry 7nkg is ON HOLD Authors: Mueller, M., Wagner, T. Description: Methyl-coenzyme M reductase from Methermicoccus shengliensis at 1.6-A resolution [[Ca...

New page

'''Unreleased structure'''

The entry 7nkg is ON HOLD

Authors: Mueller, M., Wagner, T.

Description: Methyl-coenzyme M reductase from Methermicoccus shengliensis at 1.6-A resolution
[[Category: Unreleased Structures]]
[[Category: Wagner, T]]
[[Category: Mueller, M]]