8YAA

Cryo-EM structure of MIK2-SCOOP12-BAK1

Summary for 8YAA

• Entry DOI: 10.2210/pdb8yaa/pdb
• EMDB information: 39093
• Descriptor: BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1, MDIS1-interacting receptor like kinase 2, Serine rich endogenous peptide 12, ... (7 entities in total)
• Functional Keywords: lrr-rlk, serk, mik2, scoop, bak1, plant protein, transferase, plant protein complex, transferase-plant protein complex, transferase/plant protein
• Biological source: Arabidopsis thaliana (thale cress); More
• Total number of polymer chains: 3
• Total formula weight: 99848.86

Authors

Jia, F.S.,Xiao, Y.,Chai, J.J. (deposition date: 2024-02-08, release date: 2024-10-30, Last modification date: 2025-01-01)

Primary citation

Jia, F.,Xiao, Y.,Feng, Y.,Yan, J.,Fan, M.,Sun, Y.,Huang, S.,Li, W.,Zhao, T.,Han, Z.,Hou, S.,Chai, J.
N-glycosylation facilitates the activation of a plant cell-surface receptor.
Nat.Plants, 10:2014-2026, 2024

PubMed Abstract: Plant receptor kinases (RKs) are critical for transmembrane signalling involved in various biological processes including plant immunity. MALE DISCOVERER1-INTERACTING RECEPTOR-LIKE KINASE 2 (MIK2) is a unique RK that recognizes a family of immunomodulatory peptides called SERINE-RICH ENDOGENOUS PEPTIDEs (SCOOPs) and activates pattern-triggered immunity responses. However, the precise mechanisms underlying SCOOP recognition and activation of MIK2 remain poorly understood. Here we present the cryogenic electron microscopy structure of a ternary complex consisting of the extracellular leucine-rich repeat (LRR) of MIK2 (MIK2LRR), SCOOP12 and the extracellular LRR of the co-receptor BAK1 (BAK1LRR) at a resolution of 3.34 Å. The structure reveals that a DNHH motif in MIK2LRR plays a critical role in specifically recognizing the highly conserved SxS motif of SCOOP12. Furthermore, the structure demonstrates that N-glycans at MIK2LRR directly interact with the N-terminal capping region of BAK1LRR. Mutation of the glycosylation site, MIK2LRR, completely abolishes the SCOOP12-independent interaction between MIK2LRR and BAK1LRR and substantially impairs the assembly of the MIK2LRR-SCOOP12-BAK1LRR complex. Supporting the biological relevance of N410-glycosylation, MIK2 substantially compromises SCOOP12-triggered immune responses in plants. Collectively, these findings elucidate the mechanism underlying the loose specificity of SCOOP recognition by MIK2 and reveal an unprecedented mechanism by which N-glycosylation modification of LRR-RK promotes receptor activation.

PubMed: 39511417
DOI: 10.1038/s41477-024-01841-6

Experimental method

ELECTRON MICROSCOPY (3.34 Å)