6fg7
Crystal structure of the BIR2 ectodomain from Arabidopsis thaliana.
Structural highlights
FunctionBIR2_ARATH Pseudokinases lacking protein kinase activity and unable to bind ATP-analogs (PubMed:24556575). Negative regulator of pathogen-associated molecular patterns- (PAMP-) triggered immunity by limiting BAK1-receptor complex formation in the absence of ligands (PubMed:24388849).[1] [2] Publication Abstract from PubMedThe leucine-rich repeat receptor kinase (LRR-RK) BRASSINOSTEROID INSENSITIVE 1 (BRI1) requires a shape-complementary SOMATIC EMBRYOGENESIS RECEPTOR KINASE (SERK) co-receptor for brassinosteroid sensing and receptor activation (1) . Interface mutations that weaken the interaction between receptor and co-receptor in vitro reduce brassinosteroid signalling responses (2) . The SERK3 elongated (elg) allele(3-5) maps to the complex interface and shows enhanced brassinosteroid signalling, but surprisingly no tighter binding to the BRI1 ectodomain in vitro. Here, we report that rather than promoting the interaction with BRI1, the elg mutation disrupts the ability of the co-receptor to interact with the ectodomains of BRI1-ASSOCIATED-KINASE1 INTERACTING KINASE (BIR) receptor pseudokinases, negative regulators of LRR-RK signalling (6) . A conserved lateral surface patch in BIR LRR domains is required for targeting SERK co-receptors and the elg allele maps to the core of the complex interface in a 1.25 A BIR3-SERK1 structure. Collectively, our structural, quantitative biochemical and genetic analyses suggest that brassinosteroid signalling complex formation is negatively regulated by BIR receptor ectodomains. The SERK3 elongated allele defines a role for BIR ectodomains in brassinosteroid signalling.,Hohmann U, Nicolet J, Moretti A, Hothorn LA, Hothorn M Nat Plants. 2018 May 7. pii: 10.1038/s41477-018-0150-9. doi:, 10.1038/s41477-018-0150-9. PMID:29735985[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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