6J5V

Ligand-triggered allosteric ADP release primes a plant NLR complex

6J5V の概要

• エントリーDOI: 10.2210/pdb6j5v/pdb
• EMDBエントリー: 0682
• 分子名称: Disease resistance RPP13-like protein 4, Probable serine/threonine-protein kinase PBL2, Protein kinase superfamily protein, ... (4 entities in total)
• 機能のキーワード: zar1, rks1, pbl2-ump, plant protein
• 由来する生物種: Arabidopsis thaliana (thale cress); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 184311.14

構造登録者

Wang, J.Z.,Wang, J.,Hu, M.J.,Wang, H.W.,Zhou, J.M.,Chai, J.J. (登録日: 2019-01-12, 公開日: 2019-04-03, 最終更新日: 2024-10-16)

主引用文献

Wang, J.,Wang, J.,Hu, M.,Wu, S.,Qi, J.,Wang, G.,Han, Z.,Qi, Y.,Gao, N.,Wang, H.W.,Zhou, J.M.,Chai, J.
Ligand-triggered allosteric ADP release primes a plant NLR complex.
Science, 364:-, 2019

PubMed Abstract: Pathogen recognition by nucleotide-binding (NB), leucine-rich repeat (LRR) receptors (NLRs) plays roles in plant immunity. The pv. effector AvrAC uridylylates the PBL2 kinase, and the latter (PBL2) 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 in an inactive and intermediate state, respectively. The ZAR1 domain, compared with animal NLR domains, is differently positioned to sequester ZAR1 in an inactive state. Recognition of PBL2 is exclusively through RKS1, which interacts with ZAR1 PBL2 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.

PubMed: 30948526
DOI: 10.1126/science.aav5868

実験手法

ELECTRON MICROSCOPY (4.25 Å)