8K08

Pq3-O-UGT2 with 20(S)-Ginsenoside Rh2

8K08 の概要

• エントリーDOI: 10.2210/pdb8k08/pdb
• 分子名称: Glycosyltransferase, Ginsenoside Rh2 (2 entities in total)
• 機能のキーワード: glycosytransferase, transferase
• 由来する生物種: Panax quinquefolius
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 103021.85

構造登録者

Ji, Q.S.,Liu, Y.R.,Mei, K.R. (登録日: 2023-07-07, 公開日: 2025-01-29, 最終更新日: 2025-04-02)

主引用文献

Ji, Q.,Liu, Y.,Zhang, H.,Gao, Y.,Ding, Y.,Ding, Y.,Xie, J.,Zhang, J.,Jin, X.,Lai, B.,Chen, C.,Wang, J.,Gao, W.,Mei, K.
Structural Insights into the Substrate Recognition of Ginsenoside Glycosyltransferase Pq3-O-UGT2.
Adv Sci, 12:e2413185-e2413185, 2025

PubMed Abstract: Ginsenosides are a group of tetracyclic triterpenoids with promising health benefits, consisting of ginseng aglycone attached to various glycans. Pq3-O-UGT2, an important UDP-dependent glycosyltransferase (UGT), catalyzes the production of Ginsenoside Rg3 and Rd by extending the glycan chain of Ginsenoside Rh2 and F2, respectively, with higher selectivity for F2. However, the mechanism underlying its substrate recognition remains unclear. In this study, the crystal structures of Pq3-O-UGT2 in complex with its acceptor substrates are solved. The structures revealed a Nα5-oriented acceptor binding pocket in Pq3-O-UGT2, shaped by the unique conformation of the Nα5-Nα6 linker. Hydrophobic interactions play a pivotal role in the recognition of both Rh2 and F2, while hydrogen bonds specifically aid in F2 recognition due to its additional glucose moiety. The hydrophobic nature of the acceptor binding pocket also enables Pq3-O-UGT2 to recognize flavonoids. Overall, this study provides novel insights into the substrate recognition mechanisms of ginsenoside UGTs, advancing the understanding of their function and specificity.

PubMed: 39887940
DOI: 10.1002/advs.202413185

実験手法

X-RAY DIFFRACTION (3.5 Å)