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- EMDB-30451: Cryo-EM map of RPP1 mutant in complex with ATR1 -

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Basic information

Entry
Database: EMDB / ID: EMD-30451
TitleCryo-EM map of RPP1 mutant in complex with ATR1
Map data
Sample
  • Complex: Tetrameric complex of RPP1 and ATR1
    • Complex: RPP1
    • Complex: ATR1
Function / homology
Function and homology information


effector-mediated modulation of host process by symbiont / ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase / ADP binding / defense response / host cell cytoplasm / host cell nucleus / signal transduction / extracellular region
Similarity search - Function
: / : / Avirulence protein ATR1, WY-domain / ATR1 N-terminal domain / Leucine-rich repeat 3 / Leucine Rich Repeat / C-JID domain / C-JID domain / Disease resistance protein, plants / Apoptotic protease-activating factors, helical domain ...: / : / Avirulence protein ATR1, WY-domain / ATR1 N-terminal domain / Leucine-rich repeat 3 / Leucine Rich Repeat / C-JID domain / C-JID domain / Disease resistance protein, plants / Apoptotic protease-activating factors, helical domain / NB-ARC / NB-ARC domain / TIR domain / Toll - interleukin 1 - resistance / TIR domain profile. / Toll/interleukin-1 receptor homology (TIR) domain / Toll/interleukin-1 receptor homology (TIR) domain superfamily / Leucine-rich repeat domain superfamily / Winged helix DNA-binding domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Avirulence protein ATR1 / ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress) / Hyaloperonospora arabidopsidis Emoy2 (eukaryote)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.21 Å
AuthorsMa SC / Lapin D / Liu L / Sun Y / Song W / Zhang XX / Logemann E / Yu DL / Wang J / Jirschitzka J ...Ma SC / Lapin D / Liu L / Sun Y / Song W / Zhang XX / Logemann E / Yu DL / Wang J / Jirschitzka J / Han ZF / SchulzeLefert P / Parker JE / Chai JJ
Funding support China, Germany, 2 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)31421001 for J.C. China
Alexander von Humboldt Foundation Germany
CitationJournal: Science / Year: 2020
Title: Direct pathogen-induced assembly of an NLR immune receptor complex to form a holoenzyme.
Authors: Shoucai Ma / Dmitry Lapin / Li Liu / Yue Sun / Wen Song / Xiaoxiao Zhang / Elke Logemann / Dongli Yu / Jia Wang / Jan Jirschitzka / Zhifu Han / Paul Schulze-Lefert / Jane E Parker / Jijie Chai /
Abstract: Direct or indirect recognition of pathogen-derived effectors by plant nucleotide-binding leucine-rich repeat (LRR) receptors (NLRs) initiates innate immune responses. The effector ATR1 activates the ...Direct or indirect recognition of pathogen-derived effectors by plant nucleotide-binding leucine-rich repeat (LRR) receptors (NLRs) initiates innate immune responses. The effector ATR1 activates the N-terminal Toll-interleukin-1 receptor (TIR) domain of NLR RPP1. We report a cryo-electron microscopy structure of RPP1 bound by ATR1. The structure reveals a C-terminal jelly roll/Ig-like domain (C-JID) for specific ATR1 recognition. Biochemical and functional analyses show that ATR1 binds to the C-JID and the LRRs to induce an RPP1 tetrameric assembly required for nicotinamide adenine dinucleotide hydrolase (NADase) activity. RPP1 tetramerization creates two potential active sites, each formed by an asymmetric TIR homodimer. Our data define the mechanism of direct effector recognition by a plant NLR leading to formation of a signaling-active holoenzyme.
History
DepositionAug 13, 2020-
Header (metadata) releaseDec 16, 2020-
Map releaseDec 16, 2020-
UpdateDec 16, 2020-
Current statusDec 16, 2020Processing site: PDBj / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 8
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 8
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_30451.png

Downloads & links

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Map

FileDownload / File: emd_30451.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesX (Sec.)Y (Row.)Z (Col.)
1.1 Å/pix.
x 360 pix.
= 395.244 Å		1.1 Å/pix.
x 360 pix.
= 395.244 Å		1.1 Å/pix.
x 360 pix.
= 395.244 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.0979 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 8.0 / Movie #1: 8
Minimum - Maximum-22.153624 - 47.140865
Average (Standard dev.)1.9262025e-12 (±1.0)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 395.24402 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.09791.09791.0979
M x/y/z360360360
origin x/y/z0.0000.0000.000
length x/y/z395.244395.244395.244
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ360360360
MAP C/R/S321
start NC/NR/NS000
NC/NR/NS360360360
D min/max/mean-22.15447.1410.000

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Supplemental data

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Sample components

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Entire : Tetrameric complex of RPP1 and ATR1

EntireName: Tetrameric complex of RPP1 and ATR1
Components
  • Complex: Tetrameric complex of RPP1 and ATR1
    • Complex: RPP1
    • Complex: ATR1

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Supramolecule #1: Tetrameric complex of RPP1 and ATR1

SupramoleculeName: Tetrameric complex of RPP1 and ATR1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2

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Supramolecule #2: RPP1

SupramoleculeName: RPP1 / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1
Source (natural)Organism: Arabidopsis thaliana (thale cress)
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)

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Supramolecule #3: ATR1

SupramoleculeName: ATR1 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2
Source (natural)Organism: Hyaloperonospora arabidopsidis Emoy2 (eukaryote)
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)

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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
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 23.542 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.21 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 178011
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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