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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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![]() | PLANT PROTEIN / Plant immunity / NLR / resistosome | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.6 Å | ||||||
![]() | Ouyang, S.Y. / Zhao, Y.B. / Li, Z.K. / Liu, M.X. | ||||||
Funding support | ![]()
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![]() | ![]() 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. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 803.2 KB | Display | ![]() |
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PDB format | ![]() | 650.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 1.6 MB | Display | ![]() |
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Full document | ![]() | 1.7 MB | Display | |
Data in XML | ![]() | 134 KB | Display | |
Data in CIF | ![]() | 197.8 KB | Display | |
Arichive directory | ![]() ![]() | 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 ![]() |
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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.) ![]() Gene: PGT21_019944, PGTUg99_030428 Production host: ![]() ![]() References: UniProt: A0A5B0N367 #3: Chemical | ChemComp-ATP / Has ligand of interest | Y | |
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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: ![]() |
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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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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