7XED

Crystal Structure of OsCIE1-Ubox and OsUBC8 complex

Summary for 7XED

• Entry DOI: 10.2210/pdb7xed/pdb
• Descriptor: UBC core domain-containing protein, U-box domain-containing protein 12 (3 entities in total)
• Functional Keywords: complex, ubiquitination, ubox, ligase, plant protein, transferase
• Biological source: Oryza sativa Japonica Group (Japanese rice); More
• Total number of polymer chains: 4
• Total formula weight: 50984.64

Authors

Zhang, Y.,Yu, C.Z. (deposition date: 2022-03-30, release date: 2023-10-04, Last modification date: 2024-06-19)

Primary citation

Wang, G.,Chen, X.,Yu, C.,Shi, X.,Lan, W.,Gao, C.,Yang, J.,Dai, H.,Zhang, X.,Zhang, H.,Zhao, B.,Xie, Q.,Yu, N.,He, Z.,Zhang, Y.,Wang, E.
Release of a ubiquitin brake activates OsCERK1-triggered immunity in rice.
Nature, 629:1158-1164, 2024

PubMed Abstract: Plant pattern-recognition receptors perceive microorganism-associated molecular patterns to activate immune signalling. Activation of the pattern-recognition receptor kinase CERK1 is essential for immunity, but tight inhibition of receptor kinases in the absence of pathogen is crucial to prevent autoimmunity. Here we find that the U-box ubiquitin E3 ligase OsCIE1 acts as a molecular brake to inhibit OsCERK1 in rice. During homeostasis, OsCIE1 ubiquitinates OsCERK1, reducing its kinase activity. In the presence of the microorganism-associated molecular pattern chitin, active OsCERK1 phosphorylates OsCIE1 and blocks its E3 ligase activity, thus releasing the brake and promoting immunity. Phosphorylation of a serine within the U-box of OsCIE1 prevents its interaction with E2 ubiquitin-conjugating enzymes and serves as a phosphorylation switch. This phosphorylation site is conserved in E3 ligases from plants to animals. Our work identifies a ligand-released brake that enables dynamic immune regulation.

PubMed: 38750355
DOI: 10.1038/s41586-024-07418-9

Experimental method

X-RAY DIFFRACTION (2.5 Å)