Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9GB9

Crystal structure of Lotus japonicus CERK6 kinase domain D460N

Summary for 9GB9
Entry DOI10.2210/pdb9gb9/pdb
DescriptorLysM type receptor kinase, 1,2-ETHANEDIOL, IMIDAZOLE, ... (4 entities in total)
Functional Keywordsimmunity, kinase, phosphorylation, plant protein
Biological sourceLotus japonicus
Total number of polymer chains4
Total formula weight132897.44
Authors
Simonsen, B.W.,Gysel, K.,Andersen, K.R. (deposition date: 2024-07-30, release date: 2024-11-27, Last modification date: 2025-12-24)
Primary citationTsitsikli, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.85 Å)
Structure validation

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon