7X5M

Tir-dsDNA complex, the initial binding state

7X5M の概要

• エントリーDOI: 10.2210/pdb7x5m/pdb
• EMDBエントリー: 32126
• 分子名称: DNA (5'-D(P*AP*TP*TP*AP*A)-3'), DNA (5'-D(P*AP*TP*TP*TP*A)-3'), Flax rust resistance protein, ... (4 entities in total)
• 機能のキーワード: plant innate immune receptor, nucleic acids, 2', 3'cnmp, hydrolase-dna complex, hydrolase/dna
• 由来する生物種: DNA molecule; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 50720.18

構造登録者

Tan, Y.,Xu, C.,Yu, D.,Song, W.,Wu, B.,Schulze-Lefert, P.,Chai, J. (登録日: 2022-03-05, 公開日: 2022-06-01, 最終更新日: 2025-07-02)

主引用文献

Yu, 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

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

実験手法

ELECTRON MICROSCOPY (3.42 Å)