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5a8k
From Proteopedia
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<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> | <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> | ||
| + | <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 5a8k" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:42, 10 August 2016
METHYL-COENZYME M REDUCTASE FROM METHANOTHERMOBACTER WOLFEII AT 1.4 A RESOLUTION
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Categories: Coenzyme-B sulfoethylthiotransferase | Methanothermobacter wolfeii | 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
