6fg8 | pdb_00006fg8

Crystal structure of the BIR3 - SERK1 complex from Arabidopsis thaliana.

spinqualitylabelsall models 6fg8, resolution 1.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6fg8 is a 2 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1PE, BMA, FUC, NAG, PEG Related: 4lsc, 6fg7 Gene: SERK1, At1g71830, F14O23.21, F14O23_24 (ARATH), At1g27190, T7N9.25 (ARATH) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SERK1_ARATH] Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Phosphorylates BRI1 on 'Ser-887' and CDC48 on at least one threonine residue and on 'Ser-41'. Confers embryogenic competence. Acts redundantly with SERK2 as a control point for sporophytic development controlling male gametophyte production. Involved in the brassinolide signaling pathway. Publication Abstract from PubMed The 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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