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: 2024-07-03) |
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
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