6r1h | pdb_00006r1h
Crystal structure of the LRR ectodomain of the receptor kinase SOBIR1 from Arabidopsis thaliana.
Structural highlights
FunctionSBIR1_ARATH Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Acting as a counterplayer of BIR1, promotes the activation of plant defense and cell death (PubMed:19616764). Component of the RLP23-SOBIR1-BAK1 complex that mediates NLP-triggered immunity (PubMed:27251392). Functions as an inhibitor/regulator of abscission, probably by regulating membrane trafficking during abscission (PubMed:20081191).[1] [2] [3] Publication Abstract from PubMedPlant-unique membrane receptor kinases with leucine-rich repeat (LRR) extracellular domains are key regulators of development and immune responses. Here, the 1.55 A 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 beta-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 beta-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. Crystal structure of the leucine-rich repeat ectodomain of the plant immune receptor kinase SOBIR1.,Hohmann U, Hothorn M Acta Crystallogr D Struct Biol. 2019 May 1;75(Pt 5):488-497. doi:, 10.1107/S2059798319005291. Epub 2019 Apr 29. PMID:31063151[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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