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Science. 2019 Apr 5;364(6435). pii: eaav5868. doi: 10.1126/science.aav5868.

Ligand-triggered allosteric ADP release primes a plant NLR complex.

Wang J#1,2, Wang J#2, Hu M#1, Wu S2, Qi J1, Wang G1, Han Z2, Qi Y2, Gao N2, Wang HW3, Zhou JM4, Chai J3,5,6.

Author information

1
State Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Academy of Seed Design, Chinese Academy of Sciences, 100101 Beijing, China.
2
Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, Center for Plant Biology, School of Life Sciences, Tsinghua University, 100084 Beijing, China.
3
Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, Center for Plant Biology, School of Life Sciences, Tsinghua University, 100084 Beijing, China. chaijj@tsinghua.edu.cn jmzhou@genetics.ac.cn hongweiwang@tsinghua.edu.cn.
4
State Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Academy of Seed Design, Chinese Academy of Sciences, 100101 Beijing, China. chaijj@tsinghua.edu.cn jmzhou@genetics.ac.cn hongweiwang@tsinghua.edu.cn.
5
Max Planck Institute for Plant Breeding Research, D-50829 Cologne, Germany.
6
Institute of Biochemistry, University of Cologne, Zuelpicher Str. 47, 50674 Cologne, Germany.
#
Contributed equally

Abstract

Pathogen recognition by nucleotide-binding (NB), leucine-rich repeat (LRR) receptors (NLRs) plays roles in plant immunity. The Xanthomonas campestris pv. campestris effector AvrAC uridylylates the Arabidopsis PBL2 kinase, and the latter (PBL2UMP) 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-PBL2UMP in an inactive and intermediate state, respectively. The ZAR1LRR domain, compared with animal NLRLRR domains, is differently positioned to sequester ZAR1 in an inactive state. Recognition of PBL2UMP is exclusively through RKS1, which interacts with ZAR1LRR PBL2UMP 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.

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PMID:
30948526
DOI:
10.1126/science.aav5868
[Indexed for MEDLINE]

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