5IXT

The crystal structure of the Arabidopsis receptor kinase HAESA LRR ectdomain in complex with a N-terminal extended IDA peptide hormone ligand.

5IXT の概要

• エントリーDOI: 10.2210/pdb5ixt/pdb
• 分子名称: Receptor-like protein kinase 5, Protein IDA, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• 機能のキーワード: membrane receptor kinase, peptide hormone receptor, signaling complex, plant development, organ shedding, signaling protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress); 詳細
• 細胞内の位置: Cell membrane ; Single-pass type I membrane protein : P47735; Secreted, extracellular space : Q8LAD7
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 71877.52

構造登録者

Santiago, J.,Hothorn, M. (登録日: 2016-03-23, 公開日: 2016-04-20, 最終更新日: 2024-01-10)

主引用文献

Santiago, J.,Brandt, B.,Wildhagen, M.,Hohmann, U.,Hothorn, L.A.,Butenko, M.A.,Hothorn, M.
Mechanistic insight into a peptide hormone signaling complex mediating floral organ abscission.
Elife, 5:-, 2016

PubMed Abstract: Plants constantly renew during their life cycle and thus require to shed senescent and damaged organs. Floral abscission is controlled by the leucine-rich repeat receptor kinase (LRR-RK) HAESA and the peptide hormone IDA. It is unknown how expression of IDA in the abscission zone leads to HAESA activation. Here we show that IDA is sensed directly by the HAESA ectodomain. Crystal structures of HAESA in complex with IDA reveal a hormone binding pocket that accommodates an active dodecamer peptide. A central hydroxyproline residue anchors IDA to the receptor. The HAESA co-receptor SERK1, a positive regulator of the floral abscission pathway, allows for high-affinity sensing of the peptide hormone by binding to an Arg-His-Asn motif in IDA. This sequence pattern is conserved among diverse plant peptides, suggesting that plant peptide hormone receptors may share a common ligand binding mode and activation mechanism.

PubMed: 27058169
DOI: 10.7554/eLife.15075

実験手法

X-RAY DIFFRACTION (1.94 Å)