Link to bioRxiv paper: http://biorxiv.org/cgi/content/short/2020.08.13.246413v1?rss=1 Authors: Martin, R., Qi, T., Zhang, H., Liu, F., King, M., Toth, C., Nogales, E., Staskawicz, B. J. Abstract: Plants and animals detect pathogen infection via 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 [A] resolution cryo-electron microscopy structure of the activated Roq1, an NLR native to Nicotiana benthamiana with a Toll-like interleukin-1 receptor (TIR) domain, bound to the Xanthomonas effector XopQ. 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. Copy rights belong to original authors. Visit the link for more info