6FG7

Crystal structure of the BIR2 ectodomain from Arabidopsis thaliana.

6FG7 の概要

• エントリーDOI: 10.2210/pdb6fg7/pdb
• 分子名称: Inactive LRR receptor-like serine/threonine-protein kinase BIR2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: leucine rich repeat receptor, membrane receptor, pseudokinase, ectodomain, protein binding
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56356.61

構造登録者

Hothorn, M.,Hohmann, U. (登録日: 2018-01-10, 公開日: 2018-01-24, 最終更新日: 2024-10-09)

主引用文献

Hohmann, U.,Nicolet, J.,Moretti, A.,Hothorn, L.A.,Hothorn, M.
The SERK3 elongated allele defines a role for BIR ectodomains in brassinosteroid signalling.
Nat Plants, 4:345-351, 2018

PubMed Abstract: 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. Interface mutations that weaken the interaction between receptor and co-receptor in vitro reduce brassinosteroid signalling responses. The SERK3 elongated (elg) allele 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. 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 Å BIR3-SERK1 structure. Collectively, our structural, quantitative biochemical and genetic analyses suggest that brassinosteroid signalling complex formation is negatively regulated by BIR receptor ectodomains.

PubMed: 29735985
DOI: 10.1038/s41477-018-0150-9

実験手法

X-RAY DIFFRACTION (1.9 Å)