7XJP
Cryo-EM structure of EDS1 and SAG101 with ATP-APDR
Summary for 7XJP
| Entry DOI | 10.2210/pdb7xjp/pdb | 
| EMDB information | 33233 | 
| Descriptor | Protein EDS1, Senescence-associated carboxylesterase 101, ISOPROPYL ALCOHOL, ... (5 entities in total) | 
| Functional Keywords | nlr, plant protein, plant immune signaling | 
| Biological source | Arabidopsis More  | 
| Total number of polymer chains | 2 | 
| Total formula weight | 135064.18 | 
| Authors | Huang, S.J.,Jia, A.L.,Han, Z.F.,Chai, J.J. (deposition date: 2022-04-18, release date: 2022-07-20, Last modification date: 2025-07-02)  | 
| Primary citation | Jia, 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: 35857644DOI: 10.1126/science.abq8180 PDB entries with the same primary citation  | 
| Experimental method | ELECTRON MICROSCOPY (2.71 Å)  | 
Structure validation
Download full validation report






