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Open data
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Basic information
| Entry | Database: PDB / ID: 7xx2 | |||||||||||||||||||||||||||||||||
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| Title | Cryo-EM structure of Sr35 resistosome induced by AvrSr35 R381A | |||||||||||||||||||||||||||||||||
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Keywords | PLANT PROTEIN / Plant immunity / NLR / resistosome | |||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationinnate immune response-activating signaling pathway / plant-type hypersensitive response / ADP binding / defense response to bacterium Similarity search - Function | |||||||||||||||||||||||||||||||||
| Biological species | ![]() Puccinia graminis f. sp. tritici (fungus) | |||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.6 Å | |||||||||||||||||||||||||||||||||
Authors | Ouyang, S.Y. / Zhao, Y.B. / Li, Z.K. / Liu, M.X. | |||||||||||||||||||||||||||||||||
| Funding support | China, 1items
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Citation | Journal: Sci Adv / Year: 2022Title: 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. | |||||||||||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 7xx2.cif.gz | 803.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb7xx2.ent.gz | 650.8 KB | Display | PDB format |
| PDBx/mmJSON format | 7xx2.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7xx2_validation.pdf.gz | 1.6 MB | Display | wwPDB validaton report |
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| Full document | 7xx2_full_validation.pdf.gz | 1.7 MB | Display | |
| Data in XML | 7xx2_validation.xml.gz | 132.7 KB | Display | |
| Data in CIF | 7xx2_validation.cif.gz | 201 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xx/7xx2 ftp://data.pdbj.org/pub/pdb/validation_reports/xx/7xx2 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 33498MC ![]() 7xdsC ![]() 7xe0C ![]() 7xvgC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 105392.203 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: Insect expression vector pBlueBacmsGCB1 (others) References: UniProt: S5ABD6 #2: Protein | | Mass: 66019.477 Da / Num. of mol.: 1 / Mutation: R381A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Puccinia graminis f. sp. tritici (fungus)Gene: PGT21_019944, PGTUg99_030428 Production host: ![]() References: UniProt: A0A5B0N367 #3: Chemical | ChemComp-ATP / Has ligand of interest | Y | Has protein modification | N | |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
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| Buffer solution | pH: 7.5 | ||||||||||||||||||||||||
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Microscopy | Model: FEI TITAN |
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| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1600 nm / Nominal defocus min: 1000 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
| Software | Name: PHENIX / Version: 1.19.2_4158: / Classification: refinement | ||||||||||||||||||||||||
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| EM software | Name: PHENIX / Category: model refinement | ||||||||||||||||||||||||
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 30530 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi





Puccinia graminis f. sp. tritici (fungus)
China, 1items
Citation





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FIELD EMISSION GUN