8HJO

Crystal structure of glycosyltransferase SgUGT94-289-3 in complex with UDP state 2

8HJO の概要

• エントリーDOI: 10.2210/pdb8hjo/pdb
• 分子名称: glycosyltranseferease, URIDINE-5'-DIPHOSPHATE, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total)
• 機能のキーワード: mogroside, ugt, siraitia grosvenorii, transferase
• 由来する生物種: Siraitia grosvenorii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 104100.02

構造登録者

Li, M.,Zhang, S.,Cui, S. (登録日: 2022-11-23, 公開日: 2024-05-29, 最終更新日: 2024-08-14)

主引用文献

Cui, S.,Zhang, S.,Wang, N.,Su, X.,Luo, Z.,Ma, X.,Li, M.
Structural insights into the catalytic selectivity of glycosyltransferase SgUGT94-289-3 towards mogrosides.
Nat Commun, 15:6423-6423, 2024

PubMed Abstract: Mogrosides constitute a series of natural sweeteners extracted from Siraitia grosvenorii fruits. These mogrosides are glucosylated to different degrees, with mogroside V (M5) and siamenoside I (SIA) being two mogrosides with high intensities of sweetness. SgUGT94-289-3 constitutes a uridine diphosphate (UDP)-dependent glycosyltransferase (UGT) responsible for the biosynthesis of M5 and SIA, by continuously catalyzing glucosylation on mogroside IIe (M2E) and on the subsequent intermediate mogroside products. However, the mechanism of its promiscuous substrate recognition and multiple catalytic modes remains unclear. Here, we report multiple complex structures and the enzymatic characterization of the glycosyltransferase SgUGT94-289-3. We show that SgUGT94-289-3 adopts a dual-pocket organization in its active site, which allows the two structurally distinct reactive ends of mogrosides to be presented from different pockets to the active site for glucosylation reaction, thus enabling both substrate promiscuity and catalytic regioselectivity. We further identified a structural motif that is essential to catalytic activity and regioselectivity, and generated SgUGT94-289-3 mutants with greatly improved M5/SIA production from M2E in an in vitro one-pot setup.

PubMed: 39080270
DOI: 10.1038/s41467-024-50662-w

実験手法

X-RAY DIFFRACTION (1.64 Å)