6R1H
Crystal structure of the LRR ectodomain of the receptor kinase SOBIR1 from Arabidopsis thaliana.
Summary for 6R1H
Entry DOI | 10.2210/pdb6r1h/pdb |
Descriptor | Leucine-rich repeat receptor-like serine/threonine/tyrosine-protein kinase SOBIR1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CHLORIDE ION, ... (6 entities in total) |
Functional Keywords | receptor kinase, lrr receptor, plant immunity, receptor-like protein interacting kinase, immune system |
Biological source | Arabidopsis thaliana (thale cress) |
Total number of polymer chains | 2 |
Total formula weight | 67375.84 |
Authors | Hohmann, U.,Hothorn, M. (deposition date: 2019-03-14, release date: 2019-05-08, Last modification date: 2024-10-23) |
Primary citation | Hohmann, U.,Hothorn, M. Crystal structure of the leucine-rich repeat ectodomain of the plant immune receptor kinase SOBIR1. Acta Crystallogr D Struct Biol, 75:488-497, 2019 Cited by PubMed Abstract: Plant-unique membrane receptor kinases with leucine-rich repeat (LRR) extracellular domains are key regulators of development and immune responses. Here, the 1.55 Å resolution crystal structure of the immune receptor kinase SOBIR1 from Arabidopsis is presented. The ectodomain structure reveals the presence of five LRRs sandwiched between noncanonical capping domains. The disulfide-bond-stabilized N-terminal cap harbours an unusual β-hairpin structure. The C-terminal cap features a highly positively charged linear motif which was found to be largely disordered in this structure. Size-exclusion chromatography and right-angle light-scattering experiments suggest that SOBIR1 is a monomer in solution. The protruding β-hairpin, a set of highly conserved basic residues at the inner surface of the SOBIR LRR domain and the presence of a genetic missense allele in LRR2 together suggest that the SOBIR1 ectodomain may mediate protein-protein interaction in plant immune signalling. PubMed: 31063151DOI: 10.1107/S2059798319005291 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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