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| | ==METHYL-COENZYME M REDUCTASE FROM METHANOTHERMOBACTER WOLFEII AT 1.4 A RESOLUTION== | | ==METHYL-COENZYME M REDUCTASE FROM METHANOTHERMOBACTER WOLFEII AT 1.4 A RESOLUTION== |
| - | <StructureSection load='5a8k' size='340' side='right' caption='[[5a8k]], [[Resolution|resolution]] 1.41Å' scene=''> | + | <StructureSection load='5a8k' size='340' side='right'caption='[[5a8k]], [[Resolution|resolution]] 1.41Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5a8k]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_wolfeii Methanothermobacter wolfeii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A8K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A8K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5a8k]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_wolfeii Methanothermobacter wolfeii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A8K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A8K FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=COM:1-THIOETHANESULFONIC+ACID'>COM</scene>, <scene name='pdbligand=ETX:2-ETHOXYETHANOL'>ETX</scene>, <scene name='pdbligand=F43:FACTOR+430'>F43</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TP7:COENZYME+B'>TP7</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]] 1.41Å</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=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='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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=COM:1-THIOETHANESULFONIC+ACID'>COM</scene>, <scene name='pdbligand=ETX:2-ETHOXYETHANOL'>ETX</scene>, <scene name='pdbligand=F43:FACTOR+430'>F43</scene>, <scene name='pdbligand=GL3:THIOGLYCIN'>GL3</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=SMC:S-METHYLCYSTEINE'>SMC</scene>, <scene name='pdbligand=TP7:COENZYME+B'>TP7</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a8r|5a8r]], [[5a8w|5a8w]]</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=5a8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a8k OCA], [https://pdbe.org/5a8k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a8k RCSB], [https://www.ebi.ac.uk/pdbsum/5a8k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a8k ProSAT]</span></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=5a8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a8k OCA], [http://pdbe.org/5a8k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a8k RCSB], [http://www.ebi.ac.uk/pdbsum/5a8k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a8k ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/H7CHY1_METWO H7CHY1_METWO] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Coenzyme-B sulfoethylthiotransferase]] | + | [[Category: Large Structures]] |
| | [[Category: Methanothermobacter wolfeii]] | | [[Category: Methanothermobacter wolfeii]] |
| - | [[Category: Ermler, U]] | + | [[Category: Ermler U]] |
| - | [[Category: Wagner, T]] | + | [[Category: Wagner T]] |
| - | [[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]]
| + | |
| Structural highlights
5a8k is a 6 chain structure with sequence from Methanothermobacter wolfeii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.41Å |
| Ligands: | , , , , , , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
H7CHY1_METWO
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wagner T, Kahnt J, Ermler U, Shima S. Didehydroaspartate Modification in Methyl-Coenzyme M Reductase Catalyzing Methane Formation. Angew Chem Int Ed Engl. 2016 Jul 28. doi: 10.1002/anie.201603882. PMID:27467699 doi:http://dx.doi.org/10.1002/anie.201603882
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