6J5T

Reconstitution and structure of a plant NLR resistosome conferring immunity

Summary for 6J5T

• Entry DOI: 10.2210/pdb6j5t/pdb
• EMDB information: 0680
• Descriptor: Probable serine/threonine-protein kinase PBL2, Protein kinase superfamily protein, Disease resistance RPP13-like protein 4, ... (5 entities in total)
• Functional Keywords: resistosome, plant protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress); More
• Total number of polymer chains: 15
• Total formula weight: 924011.63

Authors

Wang, J.Z.,Wang, J.,Hu, M.J.,Wang, H.W.,Zhou, J.M.,Chai, J.J. (deposition date: 2019-01-12, release date: 2019-03-20, Last modification date: 2024-10-16)

Primary citation

Wang, J.,Hu, M.,Wang, J.,Qi, J.,Han, Z.,Wang, G.,Qi, Y.,Wang, H.W.,Zhou, J.M.,Chai, J.
Reconstitution and structure of a plant NLR resistosome conferring immunity.
Science, 364:-, 2019

PubMed Abstract: Nucleotide-binding, leucine-rich repeat receptors (NLRs) perceive pathogen effectors to trigger plant immunity. Biochemical mechanisms underlying plant NLR activation have until now remained poorly understood. We reconstituted an active complex containing the coiled-coil NLR ZAR1, the pseudokinase RKS1, uridylated protein kinase PBL2, and 2'-deoxyadenosine 5'-triphosphate (dATP), demonstrating the oligomerization of the complex during immune activation. The cryo-electron microscopy structure reveals a wheel-like pentameric ZAR1 resistosome. Besides the nucleotide-binding domain, the coiled-coil domain of ZAR1 also contributes to resistosome pentamerization by forming an α-helical barrel that interacts with the leucine-rich repeat and winged-helix domains. Structural remodeling and fold switching during activation release the very N-terminal amphipathic α helix of ZAR1 to form a funnel-shaped structure that is required for the plasma membrane association, cell death triggering, and disease resistance, offering clues to the biochemical function of a plant resistosome.

PubMed: 30948527
DOI: 10.1126/science.aav5870

Experimental method

ELECTRON MICROSCOPY (3.4 Å)