9H73

Cryo-EM structure of an octameric G10-resistosome from wheat in 'back-to-back' arrangement

This is a non-PDB format compatible entry.

Summary for 9H73

• Entry DOI: 10.2210/pdb9h73/pdb
• Related: 9h2L 9h4i
• EMDB information: 51910
• Descriptor: NB-ARC domain-containing protein, ADENOSINE-5'-TRIPHOSPHATE (2 entities in total)
• Functional Keywords: resistance, g10-nlr, wheat, resistosome, plant protein
• Biological source: Triticum aestivum (bread wheat)
• Total number of polymer chains: 16
• Total formula weight: 1731321.65

Authors

Guo, G.H.,Zhao, H.,Lukoyanova, N.,Selvaraj, M.,Jones, J. (deposition date: 2024-10-25, release date: 2025-09-24, Last modification date: 2026-05-27)

Primary citation

Guo, G.,Zhao, H.,Bai, K.,Lu, J.,Wu, Q.,Lu, L.,Zhang, Y.,Dong, L.,Li, G.,Chen, Y.,Hou, Y.,Lu, P.,Li, M.,Zhang, H.,Wang, G.,Zhu, K.,Huang, B.,Cui, X.,Fu, H.,Hu, C.,Chu, Z.,Lyu, X.,Kamoun, S.,Wang, C.,Liu, Z.,Selvaraj, M.,Jones, J.D.G.
An activated wheat CC G10 -NLR immune receptor forms an octameric resistosome.
Cell, 189:2955-, 2026

PubMed Abstract: Nucleotide-binding, leucine-rich repeat (NLR) receptors are widespread intracellular immune sensors across kingdoms. Plant G10-type coiled-coil (CC)-NLRs constitute a distinct phylogenetic clade that remains poorly characterized. Here, we identified a gain-of-function mutant of wheat autoimmunity 3 (WAI3), which encodes a constitutively active CC-NLR resulting from a residue substitution in the leucine-rich repeat (LRR) domain. Cryo-electron microscopy (cryo-EM) analysis reveals that activated WAI3 assembles into a distinctive octameric resistosome. Arabidopsis RPS2, another CC-NLR, also forms an octamer, indicating a conserved structural property across monocot and dicot plants. The WAI3 resistosome induces a prolonged and sustained increase in cytosolic calcium, likely facilitated by a unique channel architecture arising from its divergent coiled-coil (CC) domain configuration. Notably, this domain arrangement may be shared by plant NLRs that lack the conserved EDVID (Glu-Asp-Val-Ile-Asp) motif in their CC domains. Together, our findings uncover a conserved yet previously uncharacterized NLR resistosome structure and provide insights into the plant immune receptor plasticity.

PubMed: 41864205
DOI: 10.1016/j.cell.2026.02.024

Experimental method

ELECTRON MICROSCOPY (3.6 Å)