7JLV

Structure of the activated Roq1 resistosome directly recognizing the pathogen effector XopQ

Summary for 7JLV

• Entry DOI: 10.2210/pdb7jlv/pdb
• EMDB information: 22381
• Descriptor: Disease resistance protein Roq1, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION (3 entities in total)
• Functional Keywords: resistosome, plant immunity, effector, lrr, tir, nb-arc, immune system
• Biological source: Nicotiana benthamiana
• Total number of polymer chains: 4
• Total formula weight: 604719.51

Authors

Martin, R.,Qi, T.,Zhang, H.,Lui, F.,King, M.,Toth, C.,Nogales, E.,Staskawicz, B.J. (deposition date: 2020-07-30, release date: 2020-12-02, Last modification date: 2024-03-06)

Primary citation

Martin, R.,Qi, T.,Zhang, H.,Liu, F.,King, M.,Toth, C.,Nogales, E.,Staskawicz, B.J.
Structure of the activated ROQ1 resistosome directly recognizing the pathogen effector XopQ.
Science, 370:-, 2020

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 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.

PubMed: 33273074
DOI: 10.1126/science.abd9993

Experimental method

ELECTRON MICROSCOPY (3.8 Å)