8HF2
Cryo-EM structure of WeiTsing
Summary for 8HF2
Entry DOI | 10.2210/pdb8hf2/pdb |
EMDB information | 34710 |
Descriptor | PRA1 family protein (1 entity in total) |
Functional Keywords | pentamer, channel, membrane protein |
Biological source | Arabidopsis thaliana (thale cress) |
Total number of polymer chains | 5 |
Total formula weight | 80019.95 |
Authors | Qin, L.,Tang, L.H.,Chen, Y.H. (deposition date: 2022-11-09, release date: 2023-06-21, Last modification date: 2025-07-02) |
Primary citation | Wang, W.,Qin, L.,Zhang, W.,Tang, L.,Zhang, C.,Dong, X.,Miao, P.,Shen, M.,Du, H.,Cheng, H.,Wang, K.,Zhang, X.,Su, M.,Lu, H.,Li, C.,Gao, Q.,Zhang, X.,Huang, Y.,Liang, C.,Zhou, J.M.,Chen, Y.H. WeiTsing, a pericycle-expressed ion channel, safeguards the stele to confer clubroot resistance. Cell, 186:2656-2671.e18, 2023 Cited by PubMed Abstract: Plant roots encounter numerous pathogenic microbes that often cause devastating diseases. One such pathogen, Plasmodiophora brassicae (Pb), causes clubroot disease and severe yield losses on cruciferous crops worldwide. Here, we report the isolation and characterization of WeiTsing (WTS), a broad-spectrum clubroot resistance gene from Arabidopsis. WTS is transcriptionally activated in the pericycle upon Pb infection to prevent pathogen colonization in the stele. Brassica napus carrying the WTS transgene displayed strong resistance to Pb. WTS encodes a small protein localized in the endoplasmic reticulum (ER), and its expression in plants induces immune responses. The cryoelectron microscopy (cryo-EM) structure of WTS revealed a previously unknown pentameric architecture with a central pore. Electrophysiology analyses demonstrated that WTS is a calcium-permeable cation-selective channel. Structure-guided mutagenesis indicated that channel activity is strictly required for triggering defenses. The findings uncover an ion channel analogous to resistosomes that triggers immune signaling in the pericycle. PubMed: 37295403DOI: 10.1016/j.cell.2023.05.023 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.14 Å) |
Structure validation
Download full validation report
