5A0Z

STRUCTURE OF CUTC CHOLINE LYASE CHOLINE FREE FORM FROM KLEBSIELLA PNEUMONIAE

5A0Z の概要

• エントリーDOI: 10.2210/pdb5a0z/pdb
• 関連するPDBエントリー: 5A0U
• 分子名称: CHOLINE TRIMETHYLAMINE LYASE (1 entity in total)
• 機能のキーワード: lyase, cutc, choline tma lyase, glycyl radical enzyme
• 由来する生物種: KLEBSIELLA PNEUMONIAE
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 356718.34

構造登録者

Kalnins, G.,Tars, K. (登録日: 2015-04-27, 公開日: 2015-07-29, 最終更新日: 2024-01-10)

主引用文献

Kalnins, G.,Kuka, J.,Grinberga, S.,Makrecka-Kuka, M.,Liepinsh, E.,Dambrova, M.,Tars, K.
Structure and Function of Cutc Choline Lyase from Human Microbiota Bacterium Klebsiella Pneumoniaee
J.Biol.Chem., 290:21732-, 2015

PubMed Abstract: CutC choline trimethylamine-lyase is an anaerobic bacterial glycyl radical enzyme (GRE) that cleaves choline to produce trimethylamine (TMA) and acetaldehyde. In humans, TMA is produced exclusively by the intestinal microbiota, and its metabolite, trimethylamine oxide, has been associated with a higher risk of cardiovascular diseases. Therefore, information about the three-dimensional structures of TMA-producing enzymes is important for microbiota-targeted drug discovery. We have cloned, expressed, and purified the CutC GRE and the activating enzyme CutD from Klebsiella pneumoniae, a representative of the human microbiota. We have determined the first crystal structures of both the choline-bound and choline-free forms of CutC and have discovered that binding of choline at the ligand-binding site triggers conformational changes in the enzyme structure, a feature that has not been observed for any other characterized GRE.

PubMed: 26187464
DOI: 10.1074/JBC.M115.670471

実験手法

X-RAY DIFFRACTION (3 Å)