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5a8r
From Proteopedia
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| - | ''' | + | {{Large structure}} |
| + | ==METHYL-COENZYME M REDUCTASE II FROM METHANOTHERMOBACTER MARBURGENSIS AT 2.15 A RESOLUTION== | ||
| + | <StructureSection load='5a8r' size='340' side='right' caption='[[5a8r]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5a8r]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_marburgensis Methanothermobacter marburgensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A8R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A8R FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COM:1-THIOETHANESULFONIC+ACID'>COM</scene>, <scene name='pdbligand=F43:FACTOR+430'>F43</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=TP7:COENZYME+B'>TP7</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGM:5-METHYL-ARGININE'>AGM</scene>, <scene name='pdbligand=DYA:DIDEHYDROASPARTATE'>DYA</scene>, <scene name='pdbligand=GL3:THIOGLYCIN'>GL3</scene>, <scene name='pdbligand=MGN:2-METHYL-GLUTAMINE'>MGN</scene>, <scene name='pdbligand=MHS:N1-METHYLATED+HISTIDINE'>MHS</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a8k|5a8k]], [[5a8w|5a8w]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Coenzyme-B_sulfoethylthiotransferase Coenzyme-B sulfoethylthiotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.4.1 2.8.4.1] </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=5a8r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a8r OCA], [http://pdbe.org/5a8r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a8r RCSB], [http://www.ebi.ac.uk/pdbsum/5a8r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a8r ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | {{Large structure}} | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/MCRX_METTM MCRX_METTM]] Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and a heterodisulfide. [[http://www.uniprot.org/uniprot/MCRZ_METTM MCRZ_METTM]] Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and a heterodisulfide. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | All methanogenic and methanotrophic archaea known to date contain methyl-coenzyme M reductase (MCR) that catalyzes the reversible reduction of methyl-coenzyme M to methane. This enzyme contains the nickel porphinoid F430 as a prosthetic group and, highly conserved, a thioglycine and four methylated amino acid residues near the active site. We describe herein the presence of a novel post-translationally modified amino acid, didehydroaspartate, adjacent to the thioglycine as revealed by mass spectrometry and high-resolution X-ray crystallography. Upon chemical reduction, the didehydroaspartate residue was converted into aspartate. Didehydroaspartate was found in MCR I and II from Methanothermobacter marburgensis and in MCR of phylogenetically distantly related Methanosarcina barkeri but not in MCR I and II of Methanothermobacter wolfeii, which indicates that didehydroaspartate is dispensable but might have a role in fine-tuning the active site to increase the catalytic efficiency. | ||
| - | + | Didehydroaspartate Modification in Methyl-Coenzyme M Reductase Catalyzing Methane Formation.,Wagner T, Kahnt J, Ermler U, Shima S Angew Chem Int Ed Engl. 2016 Jul 28. doi: 10.1002/anie.201603882. PMID:27467699<ref>PMID:27467699</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5a8r" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Coenzyme-B sulfoethylthiotransferase]] | ||
| + | [[Category: Methanothermobacter marburgensis]] | ||
| + | [[Category: Ermler, U]] | ||
[[Category: Wagner, T]] | [[Category: Wagner, T]] | ||
| - | [[Category: | + | [[Category: Binding site]] |
| + | [[Category: Catalysis]] | ||
| + | [[Category: Coenzyme]] | ||
| + | [[Category: Disulfide]] | ||
| + | [[Category: Hydrogen]] | ||
| + | [[Category: Hydrogen bonding]] | ||
| + | [[Category: Ligand]] | ||
| + | [[Category: Mesna]] | ||
| + | [[Category: Metalloporphyrin]] | ||
| + | [[Category: Methane]] | ||
| + | [[Category: Methanobacterium]] | ||
| + | [[Category: Model]] | ||
| + | [[Category: Molecular]] | ||
| + | [[Category: Nickel]] | ||
| + | [[Category: Oxidation-reduction]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Phosphothreonine]] | ||
| + | [[Category: Post-translational modification]] | ||
| + | [[Category: Protein conformation]] | ||
| + | [[Category: Protein folding]] | ||
| + | [[Category: Protein structure]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 16:14, 10 August 2016
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METHYL-COENZYME M REDUCTASE II FROM METHANOTHERMOBACTER MARBURGENSIS AT 2.15 A RESOLUTION
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Categories: Coenzyme-B sulfoethylthiotransferase | Methanothermobacter marburgensis | Ermler, U | Wagner, T | Binding site | Catalysis | Coenzyme | Disulfide | Hydrogen | Hydrogen bonding | Ligand | Mesna | Metalloporphyrin | Methane | Methanobacterium | Model | Molecular | Nickel | Oxidation-reduction | Oxidoreductase | Phosphothreonine | Post-translational modification | Protein conformation | Protein folding | Protein structure | Transferase
