8I8Z

Structure of flavone 4'-O-glucoside 7-O-glucosyltransferase from Nemophila menziesii, apo form

8I8Z の概要

• エントリーDOI: 10.2210/pdb8i8z/pdb
• 分子名称: Glycosyltransferase, SULFATE ION (3 entities in total)
• 機能のキーワード: flavone, plant protein
• 由来する生物種: Nemophila menziesii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54476.14

構造登録者

Murayama, K.,Kato-Murayama, M.,Shirouzu, M. (登録日: 2023-02-06, 公開日: 2024-02-14, 最終更新日: 2024-03-27)

主引用文献

Murayama, K.,Kato-Murayama, M.,Hosaka, T.,Okitsu, N.,Tanaka, Y.,Shirouzu, M.
Molecular basis of ligand recognition specificity of flavone glucosyltransferases in Nemophila menziesii.
Arch.Biochem.Biophys., 753:109926-109926, 2024

PubMed Abstract: Of the more than 100 families of glycosyltransferases, family 1 glycosyltransferases catalyze glycosylation using uridine diphosphate (UDP)-sugar as a sugar donor and are thus referred to as UDP-sugar:glycosyl transferases. The blue color of the Nemophila menziesii flower is derived from metalloanthocyanin, which consists of anthocyanin, flavone, and metal ions. Flavone 7-O-β-glucoside-4'-O-β-glucoside in the plant is sequentially biosynthesized from flavons by UDP-glucose:flavone 4'-O-glucosyltransferase (NmF4'GT) and UDP-glucose:flavone 4'-O-glucoside 7-O-glucosyltransferase (NmF4'G7GT). To identify the molecular mechanisms of glucosylation of flavone, the crystal structures of NmF4'G7GT in its apo form and in complex with UDP-glucose or luteolin were determined, and molecular structure prediction using AlphaFold2 was conducted for NmF4'GT. The crystal structures revealed that the size of the ligand-binding pocket and interaction environment for the glucose moiety at the pocket entrance plays a critical role in the substrate preference in NmF4'G7GT. The substrate specificity of NmF4'GT was examined by comparing its model structure with that of NmF4'G7GT. The structure of NmF4'GT may have a smaller acceptor pocket, leading to a substrate preference for non-glucosylated flavones (or flavone aglycones).

PubMed: 38346547
DOI: 10.1016/j.abb.2024.109926

実験手法

X-RAY DIFFRACTION (2.4 Å)