8PEH
Crystal structure of Lotus japonicus SYMRK kinase domain D738N
Summary for 8PEH
| Entry DOI | 10.2210/pdb8peh/pdb |
| Descriptor | Receptor-like kinase SYMRK, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | kinase, symbiosis, plant, phosphorylation, plant protein |
| Biological source | Lotus japonicus |
| Total number of polymer chains | 3 |
| Total formula weight | 102826.49 |
| Authors | Noergaard, M.M.M.,Gysel, K.,Hansen, S.B.,Andersen, K.R. (deposition date: 2023-06-14, release date: 2024-02-28, Last modification date: 2024-11-13) |
| Primary citation | Abel, N.B.,Norgaard, M.M.M.,Hansen, S.B.,Gysel, K.,Diez, I.A.,Jensen, O.N.,Stougaard, J.,Andersen, K.R. Phosphorylation of the alpha-I motif in SYMRK drives root nodule organogenesis. Proc.Natl.Acad.Sci.USA, 121:e2311522121-e2311522121, 2024 Cited by PubMed Abstract: Symbiosis receptor-like kinase SYMRK is required for root nodule symbiosis between legume plants and nitrogen-fixing bacteria. To understand symbiotic signaling from SYMRK, we determined the crystal structure to 1.95 Å and mapped the phosphorylation sites onto the intracellular domain. We identified four serine residues in a conserved "alpha-I" motif, located on the border between the kinase core domain and the flexible C-terminal tail, that, when phosphorylated, drives organogenesis. Substituting the four serines with alanines abolished symbiotic signaling, while substituting them with phosphorylation-mimicking aspartates induced the formation of spontaneous nodules in the absence of bacteria. These findings show that the signaling pathway controlling root nodule organogenesis is mediated by SYMRK phosphorylation, which may help when engineering this trait into non-legume plants. PubMed: 38363863DOI: 10.1073/pnas.2311522121 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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