5A8K

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

5A8K の概要

• エントリーDOI: 10.2210/pdb5a8k/pdb
• 関連するPDBエントリー: 5A8R 5A8W
• 分子名称: METHYL-COENZYME M REDUCTASE, MAGNESIUM ION, 1-THIOETHANESULFONIC ACID, ... (11 entities in total)
• 機能のキーワード: 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
• 由来する生物種: METHANOTHERMOBACTER WOLFEII; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 279265.16

構造登録者

Wagner, T.,Ermler, U. (登録日: 2015-07-16, 公開日: 2016-08-03, 最終更新日: 2024-01-10)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.41 Å)