7b2c: Difference between revisions
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==== | ==Crystal structure of the ethyl-coenzyme M reductase from Candidatus Ethanoperedens thermophilum gassed with xenon== | ||
<StructureSection load='7b2c' size='340' side='right'caption='[[7b2c]]' scene=''> | <StructureSection load='7b2c' size='340' side='right'caption='[[7b2c]], [[Resolution|resolution]] 1.80Å' 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'>[[7b2c]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Candidatus_Ethanoperedens_thermophilum Candidatus Ethanoperedens thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7B2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7B2C 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=7b2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b2c OCA], [https://pdbe.org/7b2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b2c RCSB], [https://www.ebi.ac.uk/pdbsum/7b2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b2c 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]] 1.8Å</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COM:1-THIOETHANESULFONIC+ACID'>COM</scene>, <scene name='pdbligand=GL3:THIOGLYCIN'>GL3</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=I2M:3-METHYL-L-ALLOISOLEUCINE'>I2M</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MGN:2-METHYL-GLUTAMINE'>MGN</scene>, <scene name='pdbligand=MHS:N1-METHYLATED+HISTIDINE'>MHS</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene>, <scene name='pdbligand=TP7:COENZYME+B'>TP7</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=USN:Dimethylated-F430+cofactor'>USN</scene>, <scene name='pdbligand=UWT:(2R)-2-[(2S)-2-[(2S)-2-oxidanylpropoxy]propoxy]propan-1-ol'>UWT</scene>, <scene name='pdbligand=XE:XENON'>XE</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=7b2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7b2c OCA], [https://pdbe.org/7b2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7b2c RCSB], [https://www.ebi.ac.uk/pdbsum/7b2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7b2c ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A7R9R6T0_9EURY A0A7R9R6T0_9EURY] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ethane, the second most abundant hydrocarbon gas in the seafloor, is efficiently oxidized by anaerobic archaea in syntrophy with sulfate-reducing bacteria. Here, we report the 0.99-angstrom-resolution structure of the proposed ethane-activating enzyme and describe the specific traits that distinguish it from methane-generating and -consuming methyl-coenzyme M reductases. The widened catalytic chamber, harboring a dimethylated nickel-containing F(430) cofactor, would adapt the chemistry of methyl-coenzyme M reductases for a two-carbon substrate. A sulfur from methionine replaces the oxygen from a canonical glutamine as the nickel lower-axial ligand, a feature conserved in thermophilic ethanotrophs. Specific loop extensions, a four-helix bundle dilatation, and posttranslational methylations result in the formation of a 33-angstrom-long hydrophobic tunnel, which guides the ethane to the buried active site as confirmed with xenon pressurization experiments. | |||
Crystal structure of a key enzyme for anaerobic ethane activation.,Hahn CJ, Lemaire ON, Kahnt J, Engilberge S, Wegener G, Wagner T Science. 2021 Jul 2;373(6550):118-121. doi: 10.1126/science.abg1765. PMID:34210888<ref>PMID:34210888</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7b2c" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Candidatus Ethanoperedens thermophilum]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Engilberge S]] | ||
[[Category: Lemaire ON]] | |||
[[Category: Wagner T]] | |||
Revision as of 12:20, 1 February 2024
Crystal structure of the ethyl-coenzyme M reductase from Candidatus Ethanoperedens thermophilum gassed with xenon
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