5FAU

wild-type choline TMA lyase in complex with choline

5FAU の概要

• エントリーDOI: 10.2210/pdb5fau/pdb
• 関連するPDBエントリー: 5FAV 5FAW 5FAY
• 分子名称: Choline trimethylamine-lyase, CHOLINE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: radical, lyase, barrel
• 由来する生物種: Desulfovibrio alaskensis (strain G20)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 381165.28

構造登録者

Funk, M.A.,Drennan, C.L. (登録日: 2015-12-12, 公開日: 2016-09-28, 最終更新日: 2023-09-27)

主引用文献

Bodea, S.,Funk, M.A.,Balskus, E.P.,Drennan, C.L.
Molecular Basis of C-N Bond Cleavage by the Glycyl Radical Enzyme Choline Trimethylamine-Lyase.
Cell Chem Biol, 23:1206-1216, 2016

PubMed Abstract: Deamination of choline catalyzed by the glycyl radical enzyme choline trimethylamine-lyase (CutC) has emerged as an important route for the production of trimethylamine, a microbial metabolite associated with both human disease and biological methane production. Here, we have determined five high-resolution X-ray structures of wild-type CutC and mechanistically informative mutants in the presence of choline. Within an unexpectedly polar active site, CutC orients choline through hydrogen bonding with a putative general base, and through close interactions between phenolic and carboxylate oxygen atoms of the protein scaffold and the polarized methyl groups of the trimethylammonium moiety. These structural data, along with biochemical analysis of active site mutants, support a mechanism that involves direct elimination of trimethylamine. This work broadens our understanding of radical-based enzyme catalysis and will aid in the rational design of inhibitors of bacterial trimethylamine production.

PubMed: 27642068
DOI: 10.1016/j.chembiol.2016.07.020

実験手法

X-RAY DIFFRACTION (1.9 Å)