7DFV

Cryo-EM structure of plant NLR RPP1 tetramer core part

7DFV の概要

• エントリーDOI: 10.2210/pdb7dfv/pdb
• EMDBエントリー: 30579
• 分子名称: NAD+ hydrolase (NADase) (1 entity in total)
• 機能のキーワード: nadase, eti, hr, plant protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 556039.12

構造登録者

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. (登録日: 2020-11-10, 公開日: 2020-12-16, 最終更新日: 2025-07-02)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (2.99 Å)