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-Structure paper
タイトル | Ligand-triggered allosteric ADP release primes a plant NLR complex. |
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ジャーナル・号・ページ | Science, Vol. 364, Issue 6435, Year 2019 |
掲載日 | 2019年4月5日 |
著者 | Jizong Wang / Jia Wang / Meijuan Hu / Shan Wu / Jinfeng Qi / Guoxun Wang / Zhifu Han / Yijun Qi / Ning Gao / Hong-Wei Wang / Jian-Min Zhou / Jijie Chai / |
PubMed 要旨 | Pathogen recognition by nucleotide-binding (NB), leucine-rich repeat (LRR) receptors (NLRs) plays roles in plant immunity. The pv. effector AvrAC uridylylates the PBL2 kinase, and the latter (PBL2) ...Pathogen recognition by nucleotide-binding (NB), leucine-rich repeat (LRR) receptors (NLRs) plays roles in plant immunity. The pv. effector AvrAC uridylylates the PBL2 kinase, and the latter (PBL2) acts as a ligand to activate the NLR ZAR1 precomplexed with the RKS1 pseudokinase. Here we report the cryo-electron microscopy structures of ZAR1-RKS1 and ZAR1-RKS1-PBL2 in an inactive and intermediate state, respectively. The ZAR1 domain, compared with animal NLR domains, is differently positioned to sequester ZAR1 in an inactive state. Recognition of PBL2 is exclusively through RKS1, which interacts with ZAR1 PBL2 binding stabilizes the RKS1 activation segment, which sterically blocks ZAR1 adenosine diphosphate (ADP) binding. This engenders a more flexible NB domain without conformational changes in the other ZAR1 domains. Our study provides a structural template for understanding plant NLRs. |
リンク | Science / PubMed:30948526 |
手法 | EM (単粒子) |
解像度 | 3.7 - 4.25 Å |
構造データ | EMDB-0681, PDB-6j5u: |
化合物 | ChemComp-U5P: ChemComp-ADP: |
由来 |
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キーワード | PLANT PROTEIN / ZAR1 / RKS1 / PBL2-UMP |