Journal: Science / Year: 2020 Title: Structure of the activated ROQ1 resistosome directly recognizing the pathogen effector XopQ. Authors: Raoul Martin / Tiancong Qi / Haibo Zhang / Furong Liu / Miles King / Claire Toth / Eva Nogales / Brian J Staskawicz / Abstract: Plants and animals detect pathogen infection using intracellular nucleotide-binding leucine-rich repeat receptors (NLRs) that directly or indirectly recognize pathogen effectors and activate an ...Plants and animals detect pathogen infection using intracellular nucleotide-binding leucine-rich repeat receptors (NLRs) that directly or indirectly recognize pathogen effectors and activate an immune response. How effector sensing triggers NLR activation remains poorly understood. Here we describe the 3.8-angstrom-resolution cryo-electron microscopy structure of the activated ROQ1 (recognition of XopQ 1), an NLR native to with a Toll-like interleukin-1 receptor (TIR) domain bound to the effector XopQ ( outer protein Q). ROQ1 directly binds to both the predicted active site and surface residues of XopQ while forming a tetrameric resistosome that brings together the TIR domains for downstream immune signaling. Our results suggest a mechanism for the direct recognition of effectors by NLRs leading to the oligomerization-dependent activation of a plant resistosome and signaling by the TIR domain.
Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 11134 Details: Images were collected as dose-fractionated movie frames.
EM imaging optics
Energyfilter name: GIF Bioquantum
-
Processing
Software
Name
Version
Classification
phenix.real_space_refine
1.18_3845
refinement
PHENIX
1.18_3845
refinement
EM software
ID
Name
Version
Category
Details
2
SerialEM
imageacquisition
4
RELION
3.1
CTFcorrection
GCTF (v1.18)
7
Coot
modelfitting
9
RELION
3.1
initialEulerassignment
10
RELION
3.1
finalEulerassignment
11
RELION
3.1
classification
12
RELION
3.1
3Dreconstruction
13
PHENIX
1.18
modelrefinement
CTF correction
Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selection
Num. of particles selected: 1254987
Symmetry
Point symmetry: C1 (asymmetric)
3D reconstruction
Resolution: 4.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 5466 / Num. of class averages: 1 / Symmetry type: POINT
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