4Z64

the plant peptide hormone receptor complex in arabidopsis

4Z64 の概要

• エントリーDOI: 10.2210/pdb4z64/pdb
• 関連するPDBエントリー: 4z5w 4z61 4z62 4z63
• 分子名称: Phytosulfokine receptor 1, Somatic embryogenesis receptor kinase 1, Phytosulfokine, ... (6 entities in total)
• 機能のキーワード: hormone receptor complex, hormone
• 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 : Q9ZVR7 Q94AG2
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 97511.56

構造登録者

Chai, J.,Wang, J.,Han, Z. (登録日: 2015-04-03, 公開日: 2016-03-02, 最終更新日: 2024-10-23)

主引用文献

Wang, J.,Li, H.,Han, Z.,Zhang, H.,Wang, T.,Lin, G.,Chang, J.,Yang, W.,Chai, J.
Allosteric receptor activation by the plant peptide hormone phytosulfokine
Nature, 525:265-268, 2015

PubMed Abstract: Phytosulfokine (PSK) is a disulfated pentapeptide that has a ubiquitous role in plant growth and development. PSK is perceived by its receptor PSKR, a leucine-rich repeat receptor kinase (LRR-RK). The mechanisms underlying the recognition of PSK, the activation of PSKR and the identity of the components downstream of the initial binding remain elusive. Here we report the crystal structures of the extracellular LRR domain of PSKR in free, PSK- and co-receptor-bound forms. The structures reveal that PSK interacts mainly with a β-strand from the island domain of PSKR, forming an anti-β-sheet. The two sulfate moieties of PSK interact directly with PSKR, sensitizing PSKR recognition of PSK. Supported by biochemical, structural and genetic evidence, PSK binding enhances PSKR heterodimerization with the somatic embryogenesis receptor-like kinases (SERKs). However, PSK is not directly involved in PSKR-SERK interaction but stabilizes PSKR island domain for recruitment of a SERK. Our data reveal the structural basis for PSKR recognition of PSK and allosteric activation of PSKR by PSK, opening up new avenues for the design of PSKR-specific small molecules.

PubMed: 26308901
DOI: 10.1038/nature14858

実験手法

X-RAY DIFFRACTION (2.659 Å)