Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis of NPR1 in activating plant immunity.
Journal, issue, pages	Nature, Vol. 605, Issue 7910, Page 561-566, Year 2022
Publish date	May 11, 2022
Authors	Shivesh Kumar / Raul Zavaliev / Qinglin Wu / Ye Zhou / Jie Cheng / Lucas Dillard / Jordan Powers / John Withers / Jinshi Zhao / Ziqiang Guan / Mario J Borgnia / Alberto Bartesaghi / Xinnian Dong / Pei Zhou /
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 ...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.
External links	Nature / PubMed:35545668 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	1.5 - 3.9 Å
Structure data	23884 7mk2 EMDB-23884, PDB-7mk2: CryoEM Structure of NPR1 Method: EM (single particle) / Resolution: 3.8 Å EMDB-23885: CryoEM Map of the NPR1-SA complex Method: EM (single particle) / Resolution: 3.9 Å EMDB-25768: Cryo-EM maps of the (TGA3)2-(NPR1)2-(TGA3)2 complex Method: EM (single particle) / Resolution: 3.6 Å 25769 7tac EMDB-25769, PDB-7tac: Cryo-EM structure of the (TGA3)2-(NPR1)2-(TGA3)2 complex Method: EM (single particle) / Resolution: 3.6 Å EMDB-25770: cryo-EM maps of the (NPR1)2-(TGA3)2 complex Method: EM (single particle) / Resolution: 3.6 Å 25771 7tad EMDB-25771, PDB-7tad: CryoEM structure of the (NPR1)2-(TGA3)2 complex Method: EM (single particle) / Resolution: 3.6 Å PDB-7mk3: Crystal structure of NPR1 Method: X-RAY DIFFRACTION / Resolution: 3.06 Å PDB-7tae: Crystal Structure of the NPR1-Interacting Domain of TGA3 Method: X-RAY DIFFRACTION / Resolution: 1.5 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-GOL: GLYCEROL ChemComp-CL: Unknown entry ChemComp-PLM: PALMITIC ACID ChemComp-HOH: WATER
Source	arabidopsis thaliana (thale cress)
Keywords	PLANT PROTEIN / IMMUNE SYSTEM / NPR1 / SAR / plant immunity / TGA3 / Plant Immunity Complex / DNA BINDING PROTEIN / NPR1-interacting domain / transcription factor