8HQB
NMR Structure of OsCIE1-Ubox
Summary for 8HQB
| Entry DOI | 10.2210/pdb8hqb/pdb |
| Related | 7XED |
| NMR Information | BMRB: 36528 |
| Descriptor | U-box domain-containing protein 12 (1 entity in total) |
| Functional Keywords | ubiquitination, ubox, ligase, plant protein |
| Biological source | Oryza sativa Japonica Group (Japanese rice) |
| Total number of polymer chains | 2 |
| Total formula weight | 17904.54 |
| Authors | |
| 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 Cited by 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: 38750355DOI: 10.1038/s41586-024-07418-9 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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