Ligand-triggered allosteric ADP release primes a plant NLR complex.

Abstract

Pathogen recognition by nucleotide-binding (NB), leucine-rich repeat (LRR) receptors (NLRs) plays roles in plant immunity. The <i>Xanthomonas campestris</i> pv. <i>campestris</i> effector AvrAC uridylylates the <i>Arabidopsis</i> PBL2 kinase, and the latter (PBL2^UMP) acts as a ligand to activate the NLR ZAR1 precomplexed with the RKS1 pseudokinase. Here we report the cryo-electron microscopy structures of ZAR1-RKS1 and ZAR1-RKS1-PBL2^UMP in an inactive and intermediate state, respectively. The ZAR1^LRR domain, compared with animal NLR^LRR domains, is differently positioned to sequester ZAR1 in an inactive state. Recognition of PBL2^UMP is exclusively through RKS1, which interacts with ZAR1^LRR PBL2^UMP binding stabilizes the RKS1 activation segment, which sterically blocks ZAR1 adenosine diphosphate (ADP) binding. This engenders a more flexible NB domain without conformational changes in the other ZAR1 domains. Our study provides a structural template for understanding plant NLRs.