7DFV

Cryo-EM structure of plant NLR RPP1 tetramer core part

Summary for 7DFV

• Entry DOI: 10.2210/pdb7dfv/pdb
• EMDB information: 30579
• Descriptor: NAD+ hydrolase (NADase) (1 entity in total)
• Functional Keywords: nadase, eti, hr, plant protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 4
• Total formula weight: 556039.12

Authors

Ma, S.C.,Lapin, D.,Liu, L.,Sun, Y.,Song, W.,Zhang, X.X.,Logemann, E.,Yu, D.L.,Wang, J.,Jirschitzka, J.,Han, Z.F.,SchulzeLefert, P.,Parker, J.E.,Chai, J.J. (deposition date: 2020-11-10, release date: 2020-12-16, Last modification date: 2024-03-27)

Primary citation

Ma, S.,Lapin, D.,Liu, L.,Sun, Y.,Song, W.,Zhang, X.,Logemann, E.,Yu, D.,Wang, J.,Jirschitzka, J.,Han, Z.,Schulze-Lefert, P.,Parker, J.E.,Chai, J.
Direct pathogen-induced assembly of an NLR immune receptor complex to form a holoenzyme.
Science, 370:-, 2020

PubMed Abstract: Direct or indirect recognition of pathogen-derived effectors by plant nucleotide-binding leucine-rich repeat (LRR) receptors (NLRs) initiates innate immune responses. The effector ATR1 activates the N-terminal Toll-interleukin-1 receptor (TIR) domain of NLR RPP1. We report a cryo-electron microscopy structure of RPP1 bound by ATR1. The structure reveals a C-terminal jelly roll/Ig-like domain (C-JID) for specific ATR1 recognition. Biochemical and functional analyses show that ATR1 binds to the C-JID and the LRRs to induce an RPP1 tetrameric assembly required for nicotinamide adenine dinucleotide hydrolase (NADase) activity. RPP1 tetramerization creates two potential active sites, each formed by an asymmetric TIR homodimer. Our data define the mechanism of direct effector recognition by a plant NLR leading to formation of a signaling-active holoenzyme.

PubMed: 33273071
DOI: 10.1126/science.abe3069

Experimental method

ELECTRON MICROSCOPY (2.99 Å)