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- EMDB-33111: SR35-LRR with AvrSR35 -

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Basic information

Entry
Database: EMDB / ID: EMD-33111
TitleSR35-LRR with AvrSR35
Map data
Sample
  • Complex: A wheat resistosome
    • Protein or peptide: Sr35_LRR and AvrSr35
Biological speciesTriticum monococcum (einkorn wheat)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.33 Å
AuthorsAlexander F / Li ET / Chai JJ
Funding support Germany, 1 items
OrganizationGrant numberCountry
Alexander von Humboldt Foundation Germany
CitationJournal: 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
DepositionMar 22, 2022-
Header (metadata) releaseSep 21, 2022-
Map releaseSep 21, 2022-
UpdateNov 2, 2022-
Current statusNov 2, 2022Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_33111.png

Downloads & links

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Map

FileDownload / File: emd_33111.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.1 Å
Density
Contour LevelBy AUTHOR: 0.015
Minimum - Maximum-0.026082912 - 0.07307145
Average (Standard dev.)4.444444e-05 (±0.0010732162)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 396.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_33111_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
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Histogram

Histogram (log scale)

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Half map: #2

Fileemd_33111_half_map_2.map
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

Histogram (log scale)

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Sample components

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Entire : A wheat resistosome

EntireName: A wheat resistosome
Components
  • Complex: A wheat resistosome
    • Protein or peptide: Sr35_LRR and AvrSr35

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Supramolecule #1: A wheat resistosome

SupramoleculeName: A wheat resistosome / type: complex / Chimera: Yes / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Triticum monococcum (einkorn wheat)
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)

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Macromolecule #1: Sr35_LRR and AvrSr35

MacromoleculeName: Sr35_LRR and AvrSr35 / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
Source (natural)Organism: Triticum monococcum (einkorn wheat)
SequenceString: MSHHFGLRKI KLLILLFLQV HGSQCAMRNF AADRVHGVES VISGSKSSSN PMALSKSMDK PDTSDLVDSN VQAKNDGSRY EEDFTAKYSE QVDHVSKILK EIEEQEPGTI IIDHKAFPIQ DKSPKQVVNF PFPKKMITES NSKDIREYLA STFPFEQQST ILDSVKSIAK ...String:
MSHHFGLRKI KLLILLFLQV HGSQCAMRNF AADRVHGVES VISGSKSSSN PMALSKSMDK PDTSDLVDSN VQAKNDGSRY EEDFTAKYSE QVDHVSKILK EIEEQEPGTI IIDHKAFPIQ DKSPKQVVNF PFPKKMITES NSKDIREYLA STFPFEQQST ILDSVKSIAK VQIDDRKAFD LQLKFRQENL AELKDQIILS LGANNGNQNW QKLLDYTNKL DELSNTKISP EEFIEEIQKV LYKVKLESTS TSKLYSQFNL SIQDFALQII HSKYKSNQIS QNDLLKLITE DEMLKILAKT KVLTYKMKYF DSASKMGINK YISTEMMDLD WQFSHYKTFN DALKKNKASD SSYLGWLTHG YSIKYGLSPN NERSMFFQDG RKYAELYAFS KSPHRKIIPG EHLKDLLAKI NKSKGIFLDQ NALLDKRIYA FHELNTLETH FPGITSSFTD DLKSNYRKKM ESVSLTCQVL QEIGNIHRFI ESKVPYHSST EYGLFSIPKI FSIPIDYKHG EKENLVSYVD FLYSTAHERI LQDNSINQLC LDPLQESLNR IKSNIPVFFN LASHSSPIKP SNVHEGKL

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.3 µm
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.33 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 476069

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