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-Structure paper
Title | Structure of the activated ROQ1 resistosome directly recognizing the pathogen effector XopQ. |
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Journal, issue, pages | Science, Vol. 370, Issue 6521, Year 2020 |
Publish date | Dec 4, 2020 |
Authors | Raoul Martin / Tiancong Qi / Haibo Zhang / Furong Liu / Miles King / Claire Toth / Eva Nogales / Brian J Staskawicz / |
PubMed 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. |
External links | Science / PubMed:33273074 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.8 - 4.6 Å |
Structure data | EMDB-22380, PDB-7jlu: EMDB-22381, PDB-7jlv: EMDB-22383, PDB-7jlx: |
Chemicals | ChemComp-CA: ChemComp-ATP: ChemComp-MG: |
Source |
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Keywords | IMMUNE SYSTEM / Resistosome / Plant Immunity / Effector / LRR / TIR / NB-ARC / PL. |