+Open data
-Basic information
Entry | Database: PDB / ID: 7xds | ||||||
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Title | Crystal structure of wheat stem rust effector AvrSr35 | ||||||
Components | AvrSr35 | ||||||
Keywords | PROTEIN TRANSPORT / Fungus / Effector / Wheat stem rust | ||||||
Function / homology | Avirulence factor Function and homology information | ||||||
Biological species | Puccinia graminis f. sp. tritici (fungus) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.06 Å | ||||||
Authors | Ouyang, S.Y. / Zhao, Y.B. | ||||||
Funding support | China, 1items
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Citation | Journal: Sci Adv / Year: 2022 Title: Pathogen effector AvrSr35 triggers Sr35 resistosome assembly via a direct recognition mechanism. Authors: Yan-Bo Zhao / Meng-Xi Liu / Tao-Tao Chen / Xiaomin Ma / Ze-Kai Li / Zichao Zheng / Si-Ru Zheng / Lifei Chen / You-Zhi Li / Li-Rui Tang / Qi Chen / Peiyi Wang / Songying Ouyang / Abstract: Nucleotide-binding, leucine-rich repeat receptors (NLRs) perceive pathogen effectors to trigger plant immunity. The direct recognition mechanism of pathogen effectors by coiled-coil NLRs (CNLs) ...Nucleotide-binding, leucine-rich repeat receptors (NLRs) perceive pathogen effectors to trigger plant immunity. The direct recognition mechanism of pathogen effectors by coiled-coil NLRs (CNLs) remains unclear. We demonstrate that the CNL Sr35 directly recognizes the pathogen effector AvrSr35 from f. sp and report a cryo-electron microscopy structure of Sr35 resistosome and a crystal structure of AvrSr35. We show that AvrSr35 forms homodimers that are disassociated into monomers upon direct recognition by the leucine-rich repeat domain of Sr35, which induces Sr35 resistosome assembly and the subsequent immune response. The first 20 amino-terminal residues of Sr35 are indispensable for immune signaling but not for plasma membrane association. Our findings reveal the direct recognition and activation mechanism of a plant CNL and provide insights into biochemical function of Sr35 resistosome. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7xds.cif.gz | 182.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7xds.ent.gz | 130.4 KB | Display | PDB format |
PDBx/mmJSON format | 7xds.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xd/7xds ftp://data.pdbj.org/pub/pdb/validation_reports/xd/7xds | HTTPS FTP |
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-Related structure data
Related structure data | 7xe0C 7xvgC 7xx2C C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 66621.438 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Puccinia graminis f. sp. tritici (fungus) Gene: PGT21_019944, PGTUg99_030428 Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria) References: UniProt: A0A5B0N367 #2: Water | ChemComp-HOH / | Has ligand of interest | Y | Has protein modification | Y | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal grow | Temperature: 289.15 K / Method: vapor diffusion, sitting drop / Details: 0.1 M sodium malonate (pH 6.0), 12% (v/v) PEG 3350 / PH range: 5.6-6.2 |
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-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL19U1 / Wavelength: 0.9792 Å |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Oct 2, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9792 Å / Relative weight: 1 |
Reflection | Resolution: 2.06→44.89 Å / Num. obs: 55016 / % possible obs: 97.8 % / Redundancy: 20 % / Biso Wilson estimate: 20.72 Å2 / Rmerge(I) obs: 0.142 / Net I/σ(I): 19 |
Reflection shell | Resolution: 2.06→2.134 Å / Rmerge(I) obs: 0.142 / Num. unique obs: 55016 |
-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 2.06→44.89 Å / SU ML: 0.2834 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 29.374 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: 29.13 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.06→44.89 Å
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Refine LS restraints |
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LS refinement shell |
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