6JTD

Crystal structure of TcCGT1 in complex with UDP

6JTD の概要

• エントリーDOI: 10.2210/pdb6jtd/pdb
• 分子名称: C-glycosyltransferase, URIDINE-5'-DIPHOSPHATE, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: c-glycosyltransferase, glycosyltransferase, transferase
• 由来する生物種: Trollius chinensis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 112438.54

構造登録者

Zhao, P.,Yun, C.H. (登録日: 2019-04-10, 公開日: 2019-06-19, 最終更新日: 2024-03-27)

主引用文献

He, J.B.,Zhao, P.,Hu, Z.M.,Liu, S.,Kuang, Y.,Zhang, M.,Li, B.,Yun, C.H.,Qiao, X.,Ye, M.
Molecular and Structural Characterization of a Promiscuous C-Glycosyltransferase from Trollius chinensis.
Angew.Chem.Int.Ed.Engl., 58:11513-11520, 2019

PubMed Abstract: Herein, the catalytic promiscuity of TcCGT1, a new C-glycosyltransferase (CGT) from the medicinal plant Trollius chinensis is explored. TcCGT1 could efficiently and regio-specifically catalyze the 8-C-glycosylation of 36 flavones and other flavonoids and could also catalyze the O-glycosylation of diverse phenolics. The crystal structure of TcCGT1 in complex with uridine diphosphate was determined at 1.85 Å resolution. Molecular docking revealed a new model for the catalytic mechanism of TcCGT1, which is initiated by the spontaneous deprotonation of the substrate. The spacious binding pocket explains the substrate promiscuity, and the binding pose of the substrate determines C- or O-glycosylation activity. Site-directed mutagenesis at two residues (I94E and G284K) switched C- to O-glycosylation. TcCGT1 is the first plant CGT with a crystal structure and the first flavone 8-C-glycosyltransferase described. This provides a basis for designing efficient glycosylation biocatalysts.

PubMed: 31163097
DOI: 10.1002/anie.201905505

実験手法

X-RAY DIFFRACTION (1.85 Å)