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9UOB

Plant-TaNNS

Summary for 9UOB
Entry DOI10.2210/pdb9uob/pdb
EMDB information64376
DescriptorProtein kinase domain-containing protein, Somatic embryogenesis receptor kinase 1, TaNNS-C (3 entities in total)
Functional Keywordscomplex, immunity, plant protein
Biological sourceTriticum aestivum (bread wheat)
More
Total number of polymer chains3
Total formula weight83944.10
Authors
Wang, L.,Zhao, J.,Yin, C.,Chi, C.,Hou, S. (deposition date: 2025-04-25, release date: 2025-12-10)
Primary citationWang, L.,Zhao, J.,Yin, C.,Li, H.,Xiao, Y.,Du, C.,Lu, Z.,Zhang, Y.,Jia, F.,Hao, J.,Yan, J.,Zhang, Y.,Li, J.,Ding, X.,Han, Z.,Cui, H.,Chai, J.,Deng, X.,Chi, C.,Hou, S.
Recognition of a phytocytokine by the DEPR1-SERK2 receptor complex confers multi-pathogen resistance in wheat.
Mol Plant, 18:1999-2017, 2025
Cited by
PubMed Abstract: The recognition of plant-derived immunogenic peptides, known as phytocytokines (PCKs), by cell surface receptors triggers immune signaling pathways that bolster basal plant defense against pathogens. However, little is known about the molecular mechanisms that underlie PCK-mediated immune regulation in wheat. In this study, we identified a wheat PCK, delta-like PCK (DEP), that robustly activates immune responses and confers multi-pathogen resistance. DEP is perceived by the leucine-rich repeat (LRR) receptor kinases (RKs) DEP RECEPTOR 1 (DEPR1) and SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE 2 (SERK2) and triggers DEPR1- and SERK2-dependent immune signaling. Cryogenic electron microscopy structural analysis revealed that DEP2 binds to the extracellular LRR domain of DEPR1 and recruits SERK2 through a disulfide-bond-stabilized loop to promote DEPR1-SERK2 heterodimerization. Furthermore, we showed that the DEP2-DEPR1-SERK2 module confers wheat resistance to Xanthomonas translucens, Fusarium graminearum, and Fusarium pseudograminearum. We also demonstrated that this module enhances wheat resistance to X. translucens by antagonizing abscisic acid signaling. Collectively, our study reveals a novel PCK-mediated immune signaling pathway and suggests a promising strategy for engineering multi-pathogen resistance in wheat.
PubMed: 41076557
DOI: 10.1016/j.molp.2025.10.005
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.33 Å)
Structure validation

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