7DRC

Cryo-EM structure of plant receptor like protein RXEG1 in complex with xyloglucanase XEG1 and BAK1

Summary for 7DRC

• Entry DOI: 10.2210/pdb7drc/pdb
• EMDB information: 30826
• Descriptor: Cell 12A endoglucanase, Membrane-localized LRR receptor-like protein, Brassinosteroid insensitive 1-associated receptor kinase 1, ... (8 entities in total)
• Functional Keywords: lrr, pti, glycoside hydrolase, inhibitor, plant protein
• Biological source: Phytophthora sojae; More
• Total number of polymer chains: 3
• Total formula weight: 163237.70

Authors

Sun, Y.,Wang, Y.,Zhang, X.X.,Chen, Z.D.,Xia, Y.Q.,Sun, Y.J.,Zhang, M.M.,Xiao, Y.,Han, Z.F.,Wang, Y.C.,Chai, J.J. (deposition date: 2020-12-27, release date: 2022-06-22, Last modification date: 2024-10-16)

Primary citation

Sun, Y.,Wang, Y.,Zhang, X.,Chen, Z.,Xia, Y.,Wang, L.,Sun, Y.,Zhang, M.,Xiao, Y.,Han, Z.,Wang, Y.,Chai, J.
Plant receptor-like protein activation by a microbial glycoside hydrolase.
Nature, 610:335-342, 2022

PubMed Abstract: Plants rely on cell-surface-localized pattern recognition receptors to detect pathogen- or host-derived danger signals and trigger an immune response. Receptor-like proteins (RLPs) with a leucine-rich repeat (LRR) ectodomain constitute a subgroup of pattern recognition receptors and play a critical role in plant immunity. Mechanisms underlying ligand recognition and activation of LRR-RLPs remain elusive. Here we report a crystal structure of the LRR-RLP RXEG1 from Nicotiana benthamiana that recognizes XEG1 xyloglucanase from the pathogen Phytophthora sojae. The structure reveals that specific XEG1 recognition is predominantly mediated by an amino-terminal and a carboxy-terminal loop-out region (RXEG1(ID)) of RXEG1. The two loops bind to the active-site groove of XEG1, inhibiting its enzymatic activity and suppressing Phytophthora infection of N. benthamiana. Binding of XEG1 promotes association of RXEG1(LRR) with the LRR-type co-receptor BAK1 through RXEG1(ID) and the last four conserved LRRs to trigger RXEG1-mediated immune responses. Comparison of the structures of apo-RXEG1(LRR), XEG1-RXEG1(LRR) and XEG1-BAK1-RXEG1(LRR) shows that binding of XEG1 induces conformational changes in the N-terminal region of RXEG1(ID) and enhances structural flexibility of the BAK1-associating regions of RXEG1(LRR). These changes allow fold switching of RXEG1(ID) for recruitment of BAK1(LRR). Our data reveal a conserved mechanism of ligand-induced heterodimerization of an LRR-RLP with BAK1 and suggest a dual function for the LRR-RLP in plant immunity.

PubMed: 36131021
DOI: 10.1038/s41586-022-05214-x

Experimental method

ELECTRON MICROSCOPY (2.92 Å)