9WP6

The cryo-EM structure of Zea mays GLN1

9WP6 の概要

• エントリーDOI: 10.2210/pdb9wp6/pdb
• EMDBエントリー: 66135
• 分子名称: Glutamine synthetase (1 entity in total)
• 機能のキーワード: chloroplast-localized;glutamine synthetase; a decameric complex, plant protein
• 由来する生物種: Zea mays
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 460828.55

構造登録者

Cheng, Y.Q.,Wu, X.X.,Zhang, Y.,Huang, Y.C. (登録日: 2025-09-08, 公開日: 2026-04-29, 最終更新日: 2026-06-24)

主引用文献

Chen, D.,Gao, L.,Li, S.,Cheng, Y.,Wu, X.,Li, W.,Zhang, J.,Fu, X.,Xiang, P.,Sun, L.,Chen, Z.,Zhang, H.,Li, Y.,Luo, S.,You, C.,Sun, L.,Huang, X.,Zhu, Y.,Zeng, X.,Wang, W.,He, Y.,Wang, H.,Zhang, Y.,Chen, X.,Wu, Y.,Huang, Y.
Plastoglobules compartmentalize nitrogen assimilation in maize.
Nature, 2026

PubMed Abstract: Efficient nitrogen assimilation is important for sustainable agriculture, yet its subcellular organization remains unknown. Here we show that plastoglobules (PGs) in the chloroplasts of mesophyll cells function as a metabolic hub that orchestrates nitrogen utilization in maize. Nitrogen-responsive dynamics of PGs represent a conserved feature across plant species. We identify two key enzymes, nitrite reductase 2 (ZmNIR2) and glutamine synthetase 1 (ZmGLN1), specifically targeted to PGs by a chloroplast transit peptide and hydrophobic region. Cryogenic electron microscopy analysis of recombinant ZmGLN1 shows a decameric complex, enabling a metabolon with ZmNIR2 for enhanced efficiency. Among two NIR and six GLN enzymes, ZmNIR2 and ZmGLN1 are the primary PG-localized components that orchestrate sub-organellar nitrogen assimilation and dictate nitrogen use efficiency. Genetic variation in ZmNIR2 splicing in cultivated germplasm generates a PG-targeted isoform (ZmNIR2) that boosts NUE. Our work establishes PGs as a central compartment for primary nitrogen assimilation, providing a promising strategy to develop high-NUE crops for global food security.

PubMed: 42236940
DOI: 10.1038/s41586-026-10610-8

実験手法

ELECTRON MICROSCOPY (1.98 Å)