7BAX
Crystal structure of LYS11 ectodomain
Summary for 7BAX
| Entry DOI | 10.2210/pdb7bax/pdb |
| Related | 7AU7 |
| Descriptor | LysM type receptor kinase, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total) |
| Functional Keywords | lysm-rlk ectodomain, plant protein |
| Biological source | Lotus japonicus |
| Total number of polymer chains | 1 |
| Total formula weight | 30074.54 |
| Authors | Laursen, M.,Cheng, J.,Gysel, K.,Blaise, M.,Andersen, K.R. (deposition date: 2020-12-16, release date: 2021-11-10, Last modification date: 2024-01-31) |
| Primary citation | Gysel, K.,Laursen, M.,Thygesen, M.B.,Lironi, D.,Bozsoki, Z.,Hjuler, C.T.,Maolanon, N.N.,Cheng, J.,Bjork, P.K.,Vinther, M.,Madsen, L.H.,Rubsam, H.,Muszynski, A.,Ghodrati, A.,Azadi, P.,Sullivan, J.T.,Ronson, C.W.,Jensen, K.J.,Blaise, M.,Radutoiu, S.,Stougaard, J.,Andersen, K.R. Kinetic proofreading of lipochitooligosaccharides determines signal activation of symbiotic plant receptors. Proc.Natl.Acad.Sci.USA, 118:-, 2021 Cited by PubMed Abstract: Plants and animals use cell surface receptors to sense and interpret environmental signals. In legume symbiosis with nitrogen-fixing bacteria, the specific recognition of bacterial lipochitooligosaccharide (LCO) signals by single-pass transmembrane receptor kinases determines compatibility. Here, we determine the structural basis for LCO perception from the crystal structures of two lysin motif receptor ectodomains and identify a hydrophobic patch in the binding site essential for LCO recognition and symbiotic function. We show that the receptor monitors the composition of the amphiphilic LCO molecules and uses kinetic proofreading to control receptor activation and signaling specificity. We demonstrate engineering of the LCO binding site to fine-tune ligand selectivity and correct binding kinetics required for activation of symbiotic signaling in plants. Finally, the hydrophobic patch is found to be a conserved structural signature in this class of LCO receptors across legumes that can be used for in silico predictions. Our results provide insights into the mechanism of cell-surface receptor activation by kinetic proofreading of ligands and highlight the potential in receptor engineering to capture benefits in plant-microbe interactions. PubMed: 34716271DOI: 10.1073/pnas.2111031118 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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