5a8k | pdb_00005a8k

METHYL-COENZYME M REDUCTASE FROM METHANOTHERMOBACTER WOLFEII AT 1.4 A RESOLUTION

spinqualitylabelsall models 5a8k, resolution 1.41Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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: AGM, CA, COM, ETX, GL3, K, MG, MGN, MHS, SMC, TP7 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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