Structure and mechanism of the heterotetrameric ADP-glucose pyrophosphorylase essential for starch synthesis in plants

heterotetrameric AGPase in apo, 3-PGA-bound, phosphate-bound, ATP/3-PGA-bound, and ADPG/3-PGA-bound states. AGPase consists of two small subunits (APS1) and two large subunits (APL1), organized as a dimer of APS1-APL1 heterodimers. Both the small and large subunits comprise an N-terminal catalytic domain and a C-terminal left-handed β-helix domain. By combining structural analysis with functional characterization, we identified the binding sites of the allosteric modulators and substrate/product in the AGPase and elucidated the mechanism of allosteric regulation, which involves 3-PGA binding-induced conformational changes at the active site. These findings provide critical insights into ADPG synthesis by plant heterotetrameric AGPase and offer clues to engineer the AGPase to enhance starch production and increase crop yields.

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Publication Details

Journal
Science Advances
Published
2026-04-01
DOI
https://doi.org/10.1126/sciadv.aeb6384
Primary Topic
Food composition and properties
Type
article
Field-Weighted Citation Impact
0.00

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article

Structure and mechanism of the heterotetrameric ADP-glucose pyrophosphorylase essential for starch synthesis in plants

Minrui Fan, Ruiying Wang, Ruiqiang Ye, Jinru Zhang et al.
Science Advances
Food composition and properties
article

Structure and mechanism of the heterotetrameric ADP-glucose pyrophosphorylase essential for starch synthesis in plants

Minrui Fan, Ruiying Wang, Ruiqiang Ye, Jinru Zhang, Hanting Yang, Xu Lin, Tianjiao Yang, Xurui Shen, Huajian Lin, Shaofeng Yi, Lizhi Zhu, Xiaojie Wang, Yutong Wu
article en

Abstract

heterotetrameric AGPase in apo, 3-PGA-bound, phosphate-bound, ATP/3-PGA-bound, and ADPG/3-PGA-bound states. AGPase consists of two small subunits (APS1) and two large subunits (APL1), organized as a dimer of APS1-APL1 heterodimers. Both the small and large subunits comprise an N-terminal catalytic domain and a C-terminal left-handed β-helix domain. By combining structural analysis with functional characterization, we identified the binding sites of the allosteric modulators and substrate/product in the AGPase and elucidated the mechanism of allosteric regulation, which involves 3-PGA binding-induced conformational changes at the active site. These findings provide critical insights into ADPG synthesis by plant heterotetrameric AGPase and offer clues to engineer the AGPase to enhance starch production and increase crop yields.

Science AdvancesVol. 12(14)
Chinese Academy of Sciences (CN), Fudan University (CN), Shanghai Institute of Organic Chemistry (CN), Center for Excellence in Molecular Plant Sciences (CN), University of Chinese Academy of Sciences (CN), State Key Laboratory of Genetic Engineering
National Natural Science Foundation of China, Chinese Academy of Sciences, China Postdoctoral Science Foundation, Fudan University, Science and Technology Commission of Shanghai Municipality
Openalex Percentile: Top 34%
Food composition and properties
DOIOpen Access PDFOpenAlex
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