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6R1H

Crystal structure of the LRR ectodomain of the receptor kinase SOBIR1 from Arabidopsis thaliana.

Summary for 6R1H
Entry DOI10.2210/pdb6r1h/pdb
DescriptorLeucine-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 Keywordsreceptor kinase, lrr receptor, plant immunity, receptor-like protein interacting kinase, immune system
Biological sourceArabidopsis thaliana (thale cress)
Total number of polymer chains2
Total formula weight67375.84
Authors
Hohmann, U.,Hothorn, M. (deposition date: 2019-03-14, release date: 2019-05-08, Last modification date: 2024-10-23)
Primary citationHohmann, 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: 31063151
DOI: 10.1107/S2059798319005291
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.55 Å)
Structure validation

237735

数据于2025-06-18公开中

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