6IJ7

Crystal Structure of Arabidopsis thaliana UGT89C1

6IJ7 の概要

• エントリーDOI: 10.2210/pdb6ij7/pdb
• 分子名称: Rhamnosyltransferase protein, GLYCEROL, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: arabidopsis thaliana, rhamnosyltransferase, rhamnoside, plant protein
• 由来する生物種: Arabidopsis thaliana
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 97159.02

構造登録者

Zong, G.,Wang, X. (登録日: 2018-10-09, 公開日: 2019-09-18, 最終更新日: 2023-11-22)

主引用文献

Zong, G.,Fei, S.,Liu, X.,Li, J.,Gao, Y.,Yang, X.,Wang, X.,Shen, Y.
Crystal structures of rhamnosyltransferase UGT89C1 from Arabidopsis thaliana reveal the molecular basis of sugar donor specificity for UDP-beta-l-rhamnose and rhamnosylation mechanism.
Plant J., 99:257-269, 2019

PubMed Abstract: Glycosylation is a key modification for most molecules including plant natural products, for example, flavonoids and isoflavonoids, and can enhance the bioactivity and bioavailability of the natural products. The crystal structure of plant rhamnosyltransferase UGT89C1 from Arabidopsis thaliana was determined, and the structures of UGT89C1 in complexes with UDP-β-l-rhamnose and acceptor quercetin revealed the detailed interactions between the enzyme and its substrates. Structural and mutational analysis indicated that Asp356, His357, Pro147 and Ile148 are key residues for sugar donor recognition and specificity for UDP-β-l-rhamnose. The mutant H357Q exhibited activity with both UDP-β-l-rhamnose and UDP-glucose. Structural comparison and mutagenesis confirmed that His21 is a key residue as the catalytic base and the only catalytic residue involved in catalysis independently as UGT89C1 lacks the other catalytic Asp that is highly conserved in other reported UGTs and forms a hydrogen bond with the catalytic base His. Ser124 is located in the corresponding position of the catalytic Asp in other UGTs and is not able to form a hydrogen bond with His21. Mutagenesis further showed that Ser124 may not be important in its catalysis, suggesting that His21 and acceptor may form an acceptor-His dyad and UGT89C1 utilizes a catalytic dyad in catalysis instead of catalytic triad. The information of structure and mutagenesis provides structural insights into rhamnosyltransferase substrate specificity and rhamnosylation mechanism.

PubMed: 30893500
DOI: 10.1111/tpj.14321

実験手法

X-RAY DIFFRACTION (2.701 Å)