7B1S

Crystal structure of the ethyl-coenzyme M reductase from Candidatus Ethanoperedens thermophilum at 0.994-A resolution

7B1S の概要

• エントリーDOI: 10.2210/pdb7b1s/pdb
• 分子名称: Ethyl-Coenzyme M reductase alpha subunit, Dimethylated-F430 cofactor, 1-THIOETHANESULFONIC ACID, ... (13 entities in total)
• 機能のキーワード: ethyl-com reductase, methyl-com reductase, ethane-oxidizers, f430-cofactor, post-translational modification, gas channel, coenzyme m, coenzyme b, true atomic resolution, thermophile, archaea., transferase
• 由来する生物種: Candidatus Ethanoperedens thermophilum; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 297856.72

構造登録者

Wagner, T.,Lemaire, O.N.,Engilberge, S. (登録日: 2020-11-25, 公開日: 2021-07-14, 最終更新日: 2024-01-31)

主引用文献

Hahn, C.J.,Lemaire, O.N.,Kahnt, J.,Engilberge, S.,Wegener, G.,Wagner, T.
Crystal structure of a key enzyme for anaerobic ethane activation.
Science, 373:118-121, 2021

PubMed Abstract: Ethane, the second most abundant hydrocarbon gas in the seafloor, is efficiently oxidized by anaerobic archaea in syntrophy with sulfate-reducing bacteria. Here, we report the 0.99-angstrom-resolution structure of the proposed ethane-activating enzyme and describe the specific traits that distinguish it from methane-generating and -consuming methyl-coenzyme M reductases. The widened catalytic chamber, harboring a dimethylated nickel-containing F cofactor, would adapt the chemistry of methyl-coenzyme M reductases for a two-carbon substrate. A sulfur from methionine replaces the oxygen from a canonical glutamine as the nickel lower-axial ligand, a feature conserved in thermophilic ethanotrophs. Specific loop extensions, a four-helix bundle dilatation, and posttranslational methylations result in the formation of a 33-angstrom-long hydrophobic tunnel, which guides the ethane to the buried active site as confirmed with xenon pressurization experiments.

PubMed: 34210888
DOI: 10.1126/science.abg1765

実験手法

X-RAY DIFFRACTION (0.992 Å)