9LB7

Crystal structure of trehalose-6-phosphate phosphorylase from Weissella ceti in complex with beta-Glc1P

Summary for 9LB7

• Entry DOI: 10.2210/pdb9lb7/pdb
• Related: 9LB6
• Descriptor: Trehalose-6-phosphate hydrolase, 1-O-phosphono-beta-D-glucopyranose, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: trehalose-6-phosphate phosphorylase, hydrolase
• Biological source: Weissella ceti
• Total number of polymer chains: 1
• Total formula weight: 86929.89

Authors

Feng, Y.,Xue, S. (deposition date: 2025-01-03, release date: 2025-07-30, Last modification date: 2025-08-06)

Primary citation

Feng, Y.,Wang, N.,Cao, Q.,Li, S.,Xu, Y.,Che, X.,Zhao, J.,Yang, C.,Xue, S.
Structural Insights into Trehalose-6-Phosphate Phosphorylase and Its Role in Trehalose 6-Phosphate Biosynthesis via a Multienzyme Cascade.
J.Agric.Food Chem., 73:19065-19075, 2025

PubMed Abstract: Trehalose 6-phosphate (Tre6P) is a critical metabolic signaling molecule in plants, orchestrating diverse biological processes, including stress resistance and photosynthetic efficiency. Recent advancements highlight its promising role in improving crop yield. However, the efficient synthesis of Tre6P remains a major challenge. Here, we identified a trehalose-6-phosphate phosphorylase WcTre6PPase from , the enzyme catalyzes the reversible synthesis of Tre6P from β-glucose 1-phosphate (βGlc1P) and glucose 6-phosphate (Glc6P), with a strong catalytic bias for Tre6P synthesis. The crystal structure of WcTre6PPase resolved in complex with βGlc1P reveals critical molecular determinants for substrate recognition and catalytic efficiency. Binding studies demonstrate a higher affinity of WcTre6PPase for βGlc1P by 1.0 ± 0.2 mM compared to Glc6P by 24.3 ± 7.1 mM. Complementary molecular docking and dynamics simulations provide detailed insights into the catalytic mechanism. Subsequently, by integrating WcTre6PPase into a novel multienzyme cascade, comprising maltose phosphorylase, polyphosphate glucokinase, and AMP/ADP-polyphosphate phosphotransferase, and optimizing reaction conditions, we achieved a remarkable Tre6P yield of 90% from maltose. This study provides molecular insights into the function of WcTre6PPase and establishes a prospective platform for Tre6P production for agricultural applications.

PubMed: 40668605
DOI: 10.1021/acs.jafc.5c05090

Experimental method

X-RAY DIFFRACTION (2.35 Å)