+Open data
-Basic information
Entry | Database: PDB / ID: 7tae | ||||||
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Title | Crystal Structure of the NPR1-Interacting Domain of TGA3 | ||||||
Components | Transcription factor TGA3 | ||||||
Keywords | DNA BINDING PROTEIN / TGA3 / NPR1-interacting domain / plant immunity / transcription factor | ||||||
Function / homology | Function and homology information systemic acquired resistance, salicylic acid mediated signaling pathway / plant-type hypersensitive response / calmodulin binding / transcription cis-regulatory region binding / defense response to bacterium / DNA-binding transcription factor activity / DNA-templated transcription / nucleus Similarity search - Function | ||||||
Biological species | Arabidopsis thaliana (thale cress) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.5 Å | ||||||
Authors | Cheng, J. / Zhou, P. | ||||||
Funding support | United States, 1items
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Citation | Journal: Nature / Year: 2022 Title: Structural basis of NPR1 in activating plant immunity. 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 / 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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7tae.cif.gz | 129.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7tae.ent.gz | 81.7 KB | Display | PDB format |
PDBx/mmJSON format | 7tae.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ta/7tae ftp://data.pdbj.org/pub/pdb/validation_reports/ta/7tae | HTTPS FTP |
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-Related structure data
Related structure data | 7mk2C 7mk3C 7tacC 7tadSC S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 28238.803 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: TGA3, BZIP22, At1g22070, F2E2.14 / Production host: Escherichia coli (E. coli) / References: UniProt: Q39234 | ||||
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#2: Chemical | ChemComp-PLM / | ||||
#3: Chemical | #4: Water | ChemComp-HOH / | Has ligand of interest | Y | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54.52 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: 10 mM HEPES (pH 8.0), 75 mM NaCl, 0.5 mM TCEP. 0.05 M sodium acetate pH 5.0, 10% (v/v) MPD 5 mg/mL protein |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9791 Å |
Detector | Type: DECTRIS EIGER2 X 16M / Detector: PIXEL / Date: Nov 24, 2021 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9791 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→47.02 Å / Num. obs: 47111 / % possible obs: 99.83 % / Redundancy: 13.2 % / Biso Wilson estimate: 26.1 Å2 / CC1/2: 0.999 / CC star: 1 / Rmerge(I) obs: 0.04796 / Rpim(I) all: 0.01372 / Rrim(I) all: 0.04993 / Net I/σ(I): 25.51 |
Reflection shell | Resolution: 1.5→1.554 Å / Num. unique obs: 4631 / CC1/2: 0.947 / CC star: 0.986 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 7TAD Resolution: 1.5→47.02 Å / SU ML: 0.1886 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 22.9478 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 34.72 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.5→47.02 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group | Refine-ID: X-RAY DIFFRACTION / Auth asym-ID: A / Label asym-ID: A
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