Related Experiment Video
Updated: May 21, 2025

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
Published on: March 11, 2022
Molecular characterization and structural basis of a promiscuous glycosyltransferase for β-(1,6) oligoglucoside chain
Zhennan Jiang1, Nianhang Chen2, Hao-Tian Wang1
1State Key Laboratory of Natural and Biomimetic Drugs, School of Pharmaceutical Sciences, Peking University, 38 Xueyuan Road, Beijing, 100191, China.
Abstract:
Sugar building blocks are crucial for the chemical diversity and biological activity of secondary metabolites. UDP-dependent glycosyltransferases (UGTs) play a pivotal role in the biosynthesis of glycosides in plants by catalysing the attachment of sugar moieties to various bioactive natural products. However, the biosynthesis of oligosaccharide-chain glycosides is often limited by the narrow substrate specificity of UGTs. In this study, we identify a regio-specific β-(1,6) glycosyltransferase, UGT94BY1, from Platycodon grandiflorum. UGT94BY1 exhibits broad substrate promiscuity and can transfer up to three sugar moieties to the C6-OH position of the glucosyl group in various triterpenoids and phenolic glycosides, thereby forming β-(1,6) oligoglucoside chains. To elucidate the mechanism underlying its substrate selectivity, we determined the crystal structure of the UGT94BY1 complex with UDP at a resolution of 2.0 Å. Molecular simulations revealed that a critical structural motif, comprising residues N84-M91, S141-L155 and R179-E186, plays a key role in recognizing sugar acceptors and facilitating chain elongation. Our study unveils a powerful glycosyltransferase for β-(1,6) oligoglucoside chain biosynthesis and highlights key regions involved in substrate recognition and sugar chain extension, providing valuable insights for designing UGTs with customized substrate specificities for biotechnological applications.
More Related Videos
05:28Demonstration of Heterologous Complexes formed by Golgi-Resident Type III Membrane Proteins using Split Luciferase Complementation Assay
Published on: September 10, 2020
11:08Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling
Published on: February 5, 2018
Related Concept Videos
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Protein Glycosylation
Glycosylation occurs in...
Proteoglycans
Protein Folding Quality Check in the RER
Glucose Transporters
Facilitated diffusion-glucose transporters (GLUTs) are encoded by the solute-linked carrier (SLC) family 2, subfamily A gene family, or SLC2A. The 14 GLUT protein members are distributed into three classes: