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7VU8

L7-Tir domain with bound ligand

Summary for 7VU8
Entry DOI10.2210/pdb7vu8/pdb
EMDB information32126
DescriptorFlax rust resistance protein, 2',3'- cyclic AMP (2 entities in total)
Functional Keywordsnucleic acid hydrolysis complex, hydrolase
Biological sourceLinum usitatissimum (Flax, Linum humile)
Total number of polymer chains1
Total formula weight23861.55
Authors
Tan, Y.,Xu, C.,Yu, D.,Song, W.,Wu, B.,Schulze-Lefert, P.,Chai, J. (deposition date: 2021-11-01, release date: 2022-06-01, Last modification date: 2024-06-26)
Primary citationYu, D.,Song, W.,Tan, E.Y.J.,Liu, L.,Cao, Y.,Jirschitzka, J.,Li, E.,Logemann, E.,Xu, C.,Huang, S.,Jia, A.,Chang, X.,Han, Z.,Wu, B.,Schulze-Lefert, P.,Chai, J.
TIR domains of plant immune receptors are 2',3'-cAMP/cGMP synthetases mediating cell death.
Cell, 185:2370-2386.e18, 2022
Cited by
PubMed Abstract: 2',3'-cAMP is a positional isomer of the well-established second messenger 3',5'-cAMP, but little is known about the biology of this noncanonical cyclic nucleotide monophosphate (cNMP). Toll/interleukin-1 receptor (TIR) domains of nucleotide-binding leucine-rich repeat (NLR) immune receptors have the NADase function necessary but insufficient to activate plant immune responses. Here, we show that plant TIR proteins, besides being NADases, act as 2',3'-cAMP/cGMP synthetases by hydrolyzing RNA/DNA. Structural data show that a TIR domain adopts distinct oligomers with mutually exclusive NADase and synthetase activity. Mutations specifically disrupting the synthetase activity abrogate TIR-mediated cell death in Nicotiana benthamiana (Nb), supporting an important role for these cNMPs in TIR signaling. Furthermore, the Arabidopsis negative regulator of TIR-NLR signaling, NUDT7, displays 2',3'-cAMP/cGMP but not 3',5'-cAMP/cGMP phosphodiesterase activity and suppresses cell death activity of TIRs in Nb. Our study identifies a family of 2',3'-cAMP/cGMP synthetases and establishes a critical role for them in plant immune responses.
PubMed: 35597242
DOI: 10.1016/j.cell.2022.04.032
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3 Å)
Structure validation

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