<table><tr><td colspan='2'>[[6j5v]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J5V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J5V FirstGlance]. <br>
<table><tr><td colspan='2'>[[6j5v]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J5V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6J5V FirstGlance]. <br>
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[[Category: Arath]]
[[Category: Arath]]
[[Category: Large Structures]]
[[Category: Large Structures]]
Revision as of 22:13, 6 March 2020
Ligand-triggered allosteric ADP release primes a plant NLR complex
6j5v is a 3 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[R13L4_ARATH] CC-NB-LRR receptor-like protein required for recognition of the Pseudomonas syringae type III effector HopZ1a. Confers allele-specific recognition and virulence attenuation of HopZ1a. Immunity mediated by ZAR1 is independent of several genes required by other resistance protein signaling pathways such as NDR1 and RAR1.[1] [PBL2_ARATH] Involved in disease resistance signaling (PubMed:20413097, PubMed:23951354). Contributes to pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) signaling and defense responses downstream of FLS2 (PubMed:20413097). Required for the bacterial XopAC/AvrAC effector-triggered immunity (ETI) against Xanthomonas campestris (PubMed:23951354).[2][3]
Publication Abstract from PubMed
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 (PBL2(UMP)) 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(UMP) in an inactive and intermediate state, respectively. The ZAR1(LRR) domain, compared with animal NLR(LRR) domains, is differently positioned to sequester ZAR1 in an inactive state. Recognition of PBL2(UMP) is exclusively through RKS1, which interacts with ZAR1(LRR) PBL2(UMP) 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.
Ligand-triggered allosteric ADP release primes a plant NLR complex.,Wang J, Wang J, Hu M, Wu S, Qi J, Wang G, Han Z, Qi Y, Gao N, Wang HW, Zhou JM, Chai J Science. 2019 Apr 5;364(6435). pii: 364/6435/eaav5868. doi:, 10.1126/science.aav5868. PMID:30948526[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Lewis JD, Wu R, Guttman DS, Desveaux D. Allele-specific virulence attenuation of the Pseudomonas syringae HopZ1a type III effector via the Arabidopsis ZAR1 resistance protein. PLoS Genet. 2010 Apr 1;6(4):e1000894. doi: 10.1371/journal.pgen.1000894. PMID:20368970 doi:http://dx.doi.org/10.1371/journal.pgen.1000894
↑ Zhang J, Li W, Xiang T, Liu Z, Laluk K, Ding X, Zou Y, Gao M, Zhang X, Chen S, Mengiste T, Zhang Y, Zhou JM. Receptor-like cytoplasmic kinases integrate signaling from multiple plant immune receptors and are targeted by a Pseudomonas syringae effector. Cell Host Microbe. 2010 Apr 22;7(4):290-301. doi: 10.1016/j.chom.2010.03.007. PMID:20413097 doi:http://dx.doi.org/10.1016/j.chom.2010.03.007
↑ Guy E, Lautier M, Chabannes M, Roux B, Lauber E, Arlat M, Noel LD. xopAC-triggered immunity against Xanthomonas depends on Arabidopsis receptor-like cytoplasmic kinase genes PBL2 and RIPK. PLoS One. 2013 Aug 9;8(8):e73469. doi: 10.1371/journal.pone.0073469. eCollection , 2013. PMID:23951354 doi:http://dx.doi.org/10.1371/journal.pone.0073469
↑ Wang J, Wang J, Hu M, Wu S, Qi J, Wang G, Han Z, Qi Y, Gao N, Wang HW, Zhou JM, Chai J. Ligand-triggered allosteric ADP release primes a plant NLR complex. Science. 2019 Apr 5;364(6435). pii: 364/6435/eaav5868. doi:, 10.1126/science.aav5868. PMID:30948526 doi:http://dx.doi.org/10.1126/science.aav5868
