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7XDD

Cryo-EM structure of EDS1 and PAD4

Summary for 7XDD
Entry DOI10.2210/pdb7xdd/pdb
EMDB information33144
DescriptorLipase-like PAD4, Protein EDS1 (2 entities in total)
Functional Keywordsnlr, plant protein, plant immune signaling, transferase-transferase activator complex, transferase/transferase activator
Biological sourceArabidopsis thaliana
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Total number of polymer chains2
Total formula weight132477.33
Authors
Huang, S.J.,Jia, A.L.,Sun, Y.,Han, Z.F.,Chai, J.J. (deposition date: 2022-03-26, release date: 2022-07-13, Last modification date: 2024-06-26)
Primary citationHuang, S.,Jia, A.,Song, W.,Hessler, G.,Meng, Y.,Sun, Y.,Xu, L.,Laessle, H.,Jirschitzka, J.,Ma, S.,Xiao, Y.,Yu, D.,Hou, J.,Liu, R.,Sun, H.,Liu, X.,Han, Z.,Chang, J.,Parker, J.E.,Chai, J.
Identification and receptor mechanism of TIR-catalyzed small molecules in plant immunity.
Science, 377:eabq3297-eabq3297, 2022
Cited by
PubMed Abstract: Plant nucleotide-binding leucine-rich repeat-containing (NLR) receptors with an N-terminal Toll/interleukin-1 receptor (TIR) domain sense pathogen effectors to enable TIR-encoded nicotinamide adenine dinucleotide hydrolase (NADase) activity for immune signaling. TIR-NLR signaling requires the helper NLRs N requirement gene 1 (NRG1), Activated Disease Resistance 1 (ADR1), and Enhanced Disease Susceptibility 1 (EDS1), which forms a heterodimer with each of its paralogs Phytoalexin Deficient 4 (PAD4) and Senescence-Associated Gene 101 (SAG101). Here, we show that TIR-containing proteins catalyze the production of 2'-(5''-phosphoribosyl)-5'-adenosine monophosphate (pRib-AMP) and diphosphate (pRib-ADP) in vitro and in planta. Biochemical and structural data demonstrate that EDS1-PAD4 is a receptor complex for pRib-AMP and pRib-ADP, which allosterically promote EDS1-PAD4 interaction with ADR1-L1 but not NRG1A. Our study identifies TIR-catalyzed pRib-AMP and pRib-ADP as a missing link in TIR signaling through EDS1-PAD4 and as likely second messengers for plant immunity.
PubMed: 35857645
DOI: 10.1126/science.abq3297
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.93 Å)
Structure validation

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