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7XOZ

Crystal structure of RPPT-TIR

Summary for 7XOZ
Entry DOI10.2210/pdb7xoz/pdb
DescriptorADP-ribosyl cyclase/cyclic ADP-ribose hydrolase, ADENOSINE-5-DIPHOSPHORIBOSE, ... (4 entities in total)
Functional Keywordsnlr, plant protein, plant immune signaling, hydrolase
Biological sourceArabidopsis thaliana (thale cress)
More
Total number of polymer chains4
Total formula weight76886.08
Authors
Song, W.,Jia, A.,Huang, S.,Chai, J. (deposition date: 2022-05-02, release date: 2023-11-08)
Primary citationJia, A.,Huang, S.,Song, W.,Wang, J.,Meng, Y.,Sun, Y.,Xu, L.,Laessle, H.,Jirschitzka, J.,Hou, J.,Zhang, T.,Yu, W.,Hessler, G.,Li, E.,Ma, S.,Yu, D.,Gebauer, J.,Baumann, U.,Liu, X.,Han, Z.,Chang, J.,Parker, J.E.,Chai, J.
TIR-catalyzed ADP-ribosylation reactions produce signaling molecules for plant immunity.
Science, 377:eabq8180-eabq8180, 2022
Cited by
PubMed Abstract: Plant pathogen-activated immune signaling by nucleotide-binding leucine-rich repeat (NLR) receptors with an N-terminal Toll/interleukin-1 receptor (TIR) domain converges on Enhanced Disease Susceptibility 1 (EDS1) and its direct partners, Phytoalexin Deficient 4 (PAD4) or Senescence-Associated Gene 101 (SAG101). TIR-encoded nicotinamide adenine dinucleotide hydrolase (NADase) produces signaling molecules to promote exclusive EDS1-PAD4 and EDS1-SAG101 interactions with helper NLR subclasses. In this work, we show that TIR-containing proteins catalyze adenosine diphosphate (ADP)-ribosylation of adenosine triphosphate (ATP) and ADP ribose (ADPR) through ADPR polymerase-like and NADase activity, forming ADP-ribosylated ATP (ADPr-ATP) and ADPr-ADPR (di-ADPR), respectively. Specific binding of ADPr-ATP or di-ADPR allosterically promotes EDS1-SAG101 interaction with helper NLR N requirement gene 1A (NRG1A) in vitro and in planta. Our data reveal an enzymatic activity of TIRs that enables specific activation of the EDS1-SAG101-NRG1 immunity branch.
PubMed: 35857644
DOI: 10.1126/science.abq8180
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.52 Å)
Structure validation

238895

数据于2025-07-16公开中

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