7MK3

Crystal structure of NPR1

7MK3 の概要

• エントリーDOI: 10.2210/pdb7mk3/pdb
• 分子名称: Regulatory protein NPR1, ZINC ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: npr1, sar, plant immunity, plant protein, immune system
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 87783.07

構造登録者

Cheng, J.,Wu, Q.,Zhou, P. (登録日: 2021-04-21, 公開日: 2022-03-16, 最終更新日: 2023-10-18)

主引用文献

Kumar, S.,Zavaliev, R.,Wu, Q.,Zhou, Y.,Cheng, J.,Dillard, L.,Powers, J.,Withers, J.,Zhao, J.,Guan, Z.,Borgnia, M.J.,Bartesaghi, A.,Dong, X.,Zhou, P.
Structural basis of NPR1 in activating plant immunity.
Nature, 605:561-566, 2022

PubMed Abstract: NPR1 is a master regulator of the defence transcriptome induced by the plant immune signal salicylic acid. Despite the important role of NPR1 in plant immunity, understanding of its regulatory mechanisms has been hindered by a lack of structural information. Here we report cryo-electron microscopy and crystal structures of Arabidopsis NPR1 and its complex with the transcription factor TGA3. Cryo-electron microscopy analysis reveals that NPR1 is a bird-shaped homodimer comprising a central Broad-complex, Tramtrack and Bric-à-brac (BTB) domain, a BTB and carboxyterminal Kelch helix bundle, four ankyrin repeats and a disordered salicylic-acid-binding domain. Crystal structure analysis reveals a unique zinc-finger motif in BTB for interacting with ankyrin repeats and mediating NPR1 oligomerization. We found that, after stimulation, salicylic-acid-induced folding and docking of the salicylic-acid-binding domain onto ankyrin repeats is required for the transcriptional cofactor activity of NPR1, providing a structural explanation for a direct role of salicylic acid in regulating NPR1-dependent gene expression. Moreover, our structure of the TGA3-NPR1-TGA3 complex, DNA-binding assay and genetic data show that dimeric NPR1 activates transcription by bridging two fatty-acid-bound TGA3 dimers to form an enhanceosome. The stepwise assembly of the NPR1-TGA complex suggests possible hetero-oligomeric complex formation with other transcription factors, revealing how NPR1 reprograms the defence transcriptome.

PubMed: 35545668
DOI: 10.1038/s41586-022-04699-w

実験手法

X-RAY DIFFRACTION (3.06 Å)