9WP6
The cryo-EM structure of Zea mays GLN1
Summary for 9WP6
| Entry DOI | 10.2210/pdb9wp6/pdb |
| EMDB information | 66135 |
| Descriptor | Glutamine synthetase (1 entity in total) |
| Functional Keywords | chloroplast-localized;glutamine synthetase; a decameric complex, plant protein |
| Biological source | Zea mays |
| Total number of polymer chains | 10 |
| Total formula weight | 460828.55 |
| Authors | Cheng, Y.Q.,Wu, X.X.,Zhang, Y.,Huang, Y.C. (deposition date: 2025-09-08, release date: 2026-04-29, Last modification date: 2026-06-24) |
| Primary citation | 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 Cited by 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: 42236940DOI: 10.1038/s41586-026-10610-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (1.98 Å) |
Structure validation
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