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7XJP

Cryo-EM structure of EDS1 and SAG101 with ATP-APDR

Summary for 7XJP
Entry DOI10.2210/pdb7xjp/pdb
EMDB information33233
DescriptorProtein EDS1, Senescence-associated carboxylesterase 101, ISOPROPYL ALCOHOL, ... (5 entities in total)
Functional Keywordsnlr, plant protein, plant immune signaling
Biological sourceArabidopsis
More
Total number of polymer chains2
Total formula weight135064.18
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 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
ELECTRON MICROSCOPY (2.71 Å)
Structure validation

226707

数据于2024-10-30公开中

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