7XDY

Crystal structure of a receptor like kinase from Arabidopsis

Summary for 7XDY

• Entry DOI: 10.2210/pdb7xdy/pdb
• Descriptor: Receptor-like protein kinase FERONIA, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: receptor-like kinase, plant protein
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 2
• Total formula weight: 71926.36

Authors

Kong, Y.Q.,Ming, Z.H. (deposition date: 2022-03-29, release date: 2023-03-29, Last modification date: 2023-11-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.28 Å)