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Yorodumi- PDB-7xc2: Cryo EM structure of oligomeric complex formed by wheat CNL Sr35 ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 7xc2 | ||||||
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Title | Cryo EM structure of oligomeric complex formed by wheat CNL Sr35 and the effector AvrSr35 of the wheat stem rust pathogen | ||||||
Components |
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Keywords | PLANT PROTEIN/INHIBITOR / LRR / CC / direct recognition / PLANT PROTEIN-INHIBITOR COMPLEX | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Triticum monococcum (einkorn wheat) Puccinia graminis f. sp. tritici (fungus) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å | ||||||
Authors | Alexander, F. / Li, E.T. / Aaron, L. / Deng, Y.N. / Sun, Y. / Chai, J.J. | ||||||
Funding support | Germany, 1items
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Citation | Journal: Nature / Year: 2022 Title: A wheat resistosome defines common principles of immune receptor channels. Authors: Alexander Förderer / Ertong Li / Aaron W Lawson / Ya-Nan Deng / Yue Sun / Elke Logemann / Xiaoxiao Zhang / Jie Wen / Zhifu Han / Junbiao Chang / Yuhang Chen / Paul Schulze-Lefert / Jijie Chai / Abstract: Plant intracellular nucleotide-binding leucine-rich repeat receptors (NLRs) detect pathogen effectors to trigger immune responses. Indirect recognition of a pathogen effector by the dicotyledonous ...Plant intracellular nucleotide-binding leucine-rich repeat receptors (NLRs) detect pathogen effectors to trigger immune responses. Indirect recognition of a pathogen effector by the dicotyledonous Arabidopsis thaliana coiled-coil domain containing NLR (CNL) ZAR1 induces the formation of a large hetero-oligomeric protein complex, termed the ZAR1 resistosome, which functions as a calcium channel required for ZAR1-mediated immunity. Whether the resistosome and channel activities are conserved among plant CNLs remains unknown. Here we report the cryo-electron microscopy structure of the wheat CNL Sr35 in complex with the effector AvrSr35 of the wheat stem rust pathogen. Direct effector binding to the leucine-rich repeats of Sr35 results in the formation of a pentameric Sr35-AvrSr35 complex, which we term the Sr35 resistosome. Wheat Sr35 and Arabidopsis ZAR1 resistosomes bear striking structural similarities, including an arginine cluster in the leucine-rich repeats domain not previously recognized as conserved, which co-occurs and forms intramolecular interactions with the 'EDVID' motif in the coiled-coil domain. Electrophysiological measurements show that the Sr35 resistosome exhibits non-selective cation channel activity. These structural insights allowed us to generate new variants of closely related wheat and barley orphan NLRs that recognize AvrSr35. Our data support the evolutionary conservation of CNL resistosomes in plants and demonstrate proof of principle for structure-based engineering of NLRs for crop improvement. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7xc2.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb7xc2.ent.gz | 884.5 KB | Display | PDB format |
PDBx/mmJSON format | 7xc2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xc/7xc2 ftp://data.pdbj.org/pub/pdb/validation_reports/xc/7xc2 | HTTPS FTP |
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-Related structure data
Related structure data | 33112MC M: map data used to model this data 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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-Components
#1: Protein | Mass: 102046.242 Da / Num. of mol.: 5 / Mutation: N151Q, I450V, I618V, I864S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Triticum monococcum (einkorn wheat) / Gene: Sr35 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: S5ABD6 #2: Protein | Mass: 50511.480 Da / Num. of mol.: 5 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Puccinia graminis f. sp. tritici (fungus) Gene: AvrSr35 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: A0A2I6B3G6 #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 |
-Sample preparation
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Source (natural) |
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Source (recombinant) |
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Buffer solution | pH: 8 | ||||||||||||||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Microscopy | Model: FEI TITAN |
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Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN |
Electron lens | Mode: DARK FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1500 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
Software | Name: PHENIX / Version: 1.15.2_3472: / Classification: refinement | ||||||||||||||||||||||||
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CTF correction | Type: NONE | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3 Å / Resolution method: FSC 0.33 CUT-OFF / Num. of particles: 230485 / Symmetry type: POINT | ||||||||||||||||||||||||
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