7XDX

Crystal structure of a receptor like kinase from Arabidopsis

7XDX の概要

• エントリーDOI: 10.2210/pdb7xdx/pdb
• 分子名称: Receptor-like protein kinase FERONIA, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: receptor-like kinase, ribosomal protein
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 71845.75

構造登録者

Kong, Y.Q.,Ming, Z.H. (登録日: 2022-03-29, 公開日: 2023-03-29, 最終更新日: 2023-11-29)

主引用文献

Kong, Y.,Chen, J.,Jiang, L.,Chen, H.,Shen, Y.,Wang, L.,Yan, Y.,Zhou, H.,Zheng, H.,Yu, F.,Ming, Z.
Structural and biochemical basis of Arabidopsis FERONIA receptor kinase-mediated early signaling initiation.
Plant Commun., 4:100559-100559, 2023

PubMed Abstract: Accumulating evidence indicates that early and essential events for receptor-like kinase (RLK) function involve both autophosphorylation and substrate phosphorylation. However, the structural and biochemical basis for these events is largely unclear. Here, we used RLK FERONIA (FER) as a model and crystallized its core kinase domain (FER-KD) and two FER-KD mutants (K565R, S525A) in complexes with ATP/ADP and Mg in the unphosphorylated state. Unphosphorylated FER-KD was found to adopt an unexpected active conformation in its crystal structure. Moreover, unphosphorylated FER-KD mutants with reduced (S525A) or no catalytic activity (K565R) also adopt similar active conformations. Biochemical studies revealed that FER-KD is a dual-specificity kinase, and its autophosphorylation is accomplished via an intermolecular mechanism. Further investigations confirmed that initiating substrate phosphorylation requires autophosphorylation of the activation segment on T696, S701, and Y704. This study reveals the structural and biochemical basis for the activation and regulatory mechanism of FER, providing a paradigm for the early steps in RLK signaling initiation.

PubMed: 36774537
DOI: 10.1016/j.xplc.2023.100559

実験手法

X-RAY DIFFRACTION (2.23 Å)