7XVG
Cryo-EM structure of binary complex of plant NLR Sr35 and effector AvrSr35
Summary for 7XVG
| Entry DOI | 10.2210/pdb7xvg/pdb |
| EMDB information | 33486 |
| Descriptor | Sr35, AvrSr35 (2 entities in total) |
| Functional Keywords | plant immunity, nlr, resistosome, plant protein |
| Biological source | Triticum monococcum More |
| Total number of polymer chains | 2 |
| Total formula weight | 156620.15 |
| Authors | Ouyang, S.Y.,Zhao, Y.B.,Li, Z.K.,Liu, M.X. (deposition date: 2022-05-23, release date: 2022-09-28, Last modification date: 2024-07-03) |
| 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 Cited by 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: 36083908DOI: 10.1126/sciadv.abq5108 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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