9GFZ

Crystal structure of Medicago Truncatula LYK3 kinase domain D459N

Summary for 9GFZ

• Entry DOI: 10.2210/pdb9gfz/pdb
• Descriptor: LysM domain receptor-like kinase 3, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (3 entities in total)
• Functional Keywords: receptor kinase, root nodule symbiosis, rlk/pelle, plant protein
• Biological source: Medicago truncatula (barrel medic)
• Total number of polymer chains: 2
• Total formula weight: 66494.30

Authors

Simonsen, B.,Gysel, K.,Andersen, C.G.,Andersen, K.R. (deposition date: 2024-08-12, release date: 2024-11-27, Last modification date: 2025-12-24)

Primary citation

Tsitsikli, M.,Simonsen, B.,Luu, T.B.,Larsen, M.M.,Andersen, C.G.,Gysel, K.,Lironi, D.,Kronauer, C.,Rubsam, H.,Hansen, S.B.,Baerentsen, R.,Wulff, J.L.,Johansen, S.H.,Sezer, G.,Stougaard, J.,Andersen, K.R.,Radutoiu, S.
Two residues reprogram immunity receptors for nitrogen-fixing symbiosis.
Nature, 648:443-450, 2025

PubMed Abstract: Receptor signalling determines cellular responses and is crucial for defining specific biological outcomes. In legume root cells, highly similar and structurally conserved chitin and Nod factor receptor kinases activate immune or symbiotic pathways, respectively, when chitinous ligands are perceived. Here we show that specific amino acid residues in the intracellular part of the Nod factor receptor NFR1 control signalling specificity and enable the distinction of immune and symbiotic responses. Functional investigation of CERK6, NFR1 and receptor variants thereof revealed a conserved motif that we term Symbiosis Determinant 1 in the juxtamembrane region of the kinase domain, which is key for symbiotic signalling. We show that two residues in Symbiosis Determinant 1 are indispensable hallmarks of NFR1-type receptors and are sufficient to convert Lotus CERK6 and barley RLK4 kinase outputs to enable symbiotic signalling in Lotus japonicus.

PubMed: 41193803
DOI: 10.1038/s41586-025-09696-3

Experimental method

X-RAY DIFFRACTION (2.5 Å)