6JTD

Crystal structure of TcCGT1 in complex with UDP

Summary for 6JTD

• Entry DOI: 10.2210/pdb6jtd/pdb
• Descriptor: C-glycosyltransferase, URIDINE-5'-DIPHOSPHATE, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: c-glycosyltransferase, glycosyltransferase, transferase
• Biological source: Trollius chinensis
• Total number of polymer chains: 2
• Total formula weight: 112438.54

Authors

Zhao, P.,Yun, C.H. (deposition date: 2019-04-10, release date: 2019-06-19, Last modification date: 2024-03-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.85 Å)