8I94
Structure of flavone 4'-O-glucoside 7-O-glucosyltransferase from Nemophila menziesii, complex with luteolin
8I94 の概要
| エントリーDOI | 10.2210/pdb8i94/pdb |
| 分子名称 | Glycosyltransferase, 2-(3,4-dihydroxyphenyl)-5,7-dihydroxy-4H-chromen-4-one, SULFATE ION, ... (4 entities in total) |
| 機能のキーワード | flavone, luteolin, plant protein |
| 由来する生物種 | Nemophila menziesii |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 109524.75 |
| 構造登録者 | |
| 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 Cited by 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: 38346547DOI: 10.1016/j.abb.2024.109926 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.43 Å) |
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