2ACV

Crystal Structure of Medicago truncatula UGT71G1

2ACV の概要

• エントリーDOI: 10.2210/pdb2acv/pdb
• 分子名称: triterpene UDP-glucosyl transferase UGT71G1, URIDINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: glycosyltransferase, udp, transferase
• 由来する生物種: Medicago truncatula (barrel medic)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 104079.11

構造登録者

Shao, H.,He, X.,Achnine, L.,Blount, J.W.,Dixon, R.A.,Wang, X. (登録日: 2005-07-19, 公開日: 2005-11-15, 最終更新日: 2024-02-14)

主引用文献

Shao, H.,He, X.,Achnine, L.,Blount, J.W.,Dixon, R.A.,Wang, X.
Crystal Structures of a Multifunctional Triterpene/Flavonoid Glycosyltransferase from Medicago truncatula.
Plant Cell, 17:3141-3154, 2005

PubMed Abstract: Glycosylation is a ubiquitous reaction controlling the bioactivity and storage of plant natural products. Glycosylation of small molecules is catalyzed by a superfamily of glycosyltransferases (GTs) in most plant species studied to date. We present crystal structures of the UDP flavonoid/triterpene GT UGT71G1 from Medicago truncatula bound to UDP or UDP-glucose. The structures reveal the key residues involved in the recognition of donor substrate and, by comparison with other GT structures, suggest His-22 as the catalytic base and Asp-121 as a key residue that may assist deprotonation of the acceptor by forming an electron transfer chain with the catalytic base. Mutagenesis confirmed the roles of these key residues in donor substrate binding and enzyme activity. Our results provide an initial structural basis for understanding the complex substrate specificity and regiospecificity underlying the glycosylation of plant natural products and other small molecules. This information will direct future attempts to engineer bioactive compounds in crop plants to improve plant, animal, and human health and to facilitate the rational design of GTs to improve the storage and stability of novel engineered bioactive compounds.

PubMed: 16214900
DOI: 10.1105/tpc.105.035055

実験手法

X-RAY DIFFRACTION (2 Å)