5A8K

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

Summary for 5A8K

• Entry DOI: 10.2210/pdb5a8k/pdb
• Related: 5A8R 5A8W
• Descriptor: METHYL-COENZYME M REDUCTASE, MAGNESIUM ION, 1-THIOETHANESULFONIC ACID, ... (11 entities in total)
• Functional Keywords: transferase, post-translational modification, binding sites, catalysis, coenzymes, disulfides, hydrogen, hydrogen bonding, ligands, mesna, metalloporphyrins, methane, methanobacterium, models, molecular, nickel, oxidation-reduction, oxidoreductases, phosphothreonine, protein conformation, protein folding, protein structure
• Biological source: METHANOTHERMOBACTER WOLFEII; More
• Total number of polymer chains: 6
• Total formula weight: 279265.16

Authors

Wagner, T.,Ermler, U. (deposition date: 2015-07-16, release date: 2016-08-03, Last modification date: 2024-01-10)

Primary citation

Wagner, T.,Kahnt, J.,Ermler, U.,Shima, S.
Didehydroaspartate Modification in Methyl-Coenzyme M Reductase Catalyzing Methane Formation.
Angew.Chem.Int.Ed.Engl., 55:10630-, 2016

PubMed Abstract: 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.

PubMed: 27467699
DOI: 10.1002/ANIE.201603882

Experimental method

X-RAY DIFFRACTION (1.41 Å)