7XE0

Cryo-EM structure of plant NLR Sr35 resistosome

Summary for 7XE0

• Entry DOI: 10.2210/pdb7xe0/pdb
• EMDB information: 33153
• Descriptor: Sr35, AvrSr35, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• Functional Keywords: plant immunity, nlr, resistosome, plant protein
• Biological source: Triticum monococcum (bread wheat); More
• Total number of polymer chains: 10
• Total formula weight: 860024.85

Authors

Ouyang, S.Y.,Zhao, Y.B.,Li, Z.K.,Liu, M.X. (deposition date: 2022-03-29, release date: 2022-09-28, Last modification date: 2025-07-02)

Primary citation

Zhao, Y.B.,Liu, M.X.,Chen, T.T.,Ma, X.,Li, Z.K.,Zheng, Z.,Zheng, S.R.,Chen, L.,Li, Y.Z.,Tang, L.R.,Chen, Q.,Wang, P.,Ouyang, S.
Pathogen effector AvrSr35 triggers Sr35 resistosome assembly via a direct recognition mechanism.
Sci Adv, 8:eabq5108-eabq5108, 2022

PubMed Abstract: Nucleotide-binding, leucine-rich repeat receptors (NLRs) perceive pathogen effectors to trigger plant immunity. The direct recognition mechanism of pathogen effectors by coiled-coil NLRs (CNLs) remains unclear. We demonstrate that the CNL Sr35 directly recognizes the pathogen effector AvrSr35 from f. sp and report a cryo-electron microscopy structure of Sr35 resistosome and a crystal structure of AvrSr35. We show that AvrSr35 forms homodimers that are disassociated into monomers upon direct recognition by the leucine-rich repeat domain of Sr35, which induces Sr35 resistosome assembly and the subsequent immune response. The first 20 amino-terminal residues of Sr35 are indispensable for immune signaling but not for plasma membrane association. Our findings reveal the direct recognition and activation mechanism of a plant CNL and provide insights into biochemical function of Sr35 resistosome.

PubMed: 36083908
DOI: 10.1126/sciadv.abq5108

Experimental method

ELECTRON MICROSCOPY (3.33 Å)