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6XWE

Crystal structure of LYK3 ectodomain

Summary for 6XWE
Entry DOI10.2210/pdb6xwe/pdb
DescriptorLysM domain receptor-like kinase 3, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
Functional Keywordslysm, receptor, symbiosis, plant protein
Biological sourceMedicago truncatula (Barrel medic)
Total number of polymer chains1
Total formula weight25264.40
Authors
Gysel, K.,Blaise, M.,Andersen, K.R. (deposition date: 2020-01-23, release date: 2020-08-12, Last modification date: 2024-10-23)
Primary citationBozsoki, Z.,Gysel, K.,Hansen, S.B.,Lironi, D.,Kronauer, C.,Feng, F.,de Jong, N.,Vinther, M.,Kamble, M.,Thygesen, M.B.,Engholm, E.,Kofoed, C.,Fort, S.,Sullivan, J.T.,Ronson, C.W.,Jensen, K.J.,Blaise, M.,Oldroyd, G.,Stougaard, J.,Andersen, K.R.,Radutoiu, S.
Ligand-recognizing motifs in plant LysM receptors are major determinants of specificity.
Science, 369:663-670, 2020
Cited by
PubMed Abstract: Plants evolved lysine motif (LysM) receptors to recognize and parse microbial elicitors and drive intracellular signaling to limit or facilitate microbial colonization. We investigated how chitin and nodulation (Nod) factor receptors of initiate differential signaling of immunity or root nodule symbiosis. Two motifs in the LysM1 domains of these receptors determine specific recognition of ligands and discriminate between their in planta functions. These motifs define the ligand-binding site and make up the most structurally divergent regions in cognate Nod factor receptors. An adjacent motif modulates the specificity for Nod factor recognition and determines the selection of compatible rhizobial symbionts in legumes. We also identified how binding specificities in LysM receptors can be altered to facilitate Nod factor recognition and signaling from a chitin receptor, advancing the prospects of engineering rhizobial symbiosis into nonlegumes.
PubMed: 32764065
DOI: 10.1126/science.abb3377
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.49 Å)
Structure validation

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