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| | <SX load='6j5w' size='340' side='right' viewer='molstar' caption='[[6j5w]], [[Resolution|resolution]] 3.70Å' scene=''> | | <SX load='6j5w' size='340' side='right' viewer='molstar' caption='[[6j5w]], [[Resolution|resolution]] 3.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6j5w]] is a 2 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=6J5W OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6J5W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6j5w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6J5W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6J5W FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At3g57710 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH]), RPP13L4, ZAR1, At3g50950, F18B3.230 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6j5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j5w OCA], [http://pdbe.org/6j5w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6j5w RCSB], [http://www.ebi.ac.uk/pdbsum/6j5w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6j5w ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6j5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6j5w OCA], [https://pdbe.org/6j5w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6j5w RCSB], [https://www.ebi.ac.uk/pdbsum/6j5w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6j5w ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/R13L4_ARATH 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.<ref>PMID:20368970</ref> | + | [https://www.uniprot.org/uniprot/ZRK1_ARATH ZRK1_ARATH] Serine/threonine-protein kinase that confers a broad-spectrum quantitative disease resistance (QDR) to the pathogenic biotrophic bacteria Xanthomonas campestris (e.g. pv. campestris (Xcc), pv. raphani, pv. armoriaceae and pv. incanae) by restricting bacterial spread to the vascular system from the infection site; X.campestris causes black rot disease in crops (PubMed:24068949, PubMed:26355215, PubMed:30948526). Seems to not have any kinase activity (PubMed:24068949).<ref>PMID:24068949</ref> <ref>PMID:26355215</ref> <ref>PMID:30948526</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == 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<ref>PMID:30948526</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div> | + | |
| - | <div class="pdbe-citations 6j5w" style="background-color:#fffaf0;"></div> | + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chai, J J]] | + | [[Category: Chai JJ]] |
| - | [[Category: Hu, M J]] | + | [[Category: Hu MJ]] |
| - | [[Category: Wang, H W]] | + | [[Category: Wang HW]] |
| - | [[Category: Wang, J]] | + | [[Category: Wang J]] |
| - | [[Category: Wang, J Z]] | + | [[Category: Wang JZ]] |
| - | [[Category: Zhou, J M]] | + | [[Category: Zhou JM]] |
| - | [[Category: Plant protein]]
| + | |
| - | [[Category: Rks1]]
| + | |
| - | [[Category: Zar1]]
| + | |
| Structural highlights
Function
ZRK1_ARATH Serine/threonine-protein kinase that confers a broad-spectrum quantitative disease resistance (QDR) to the pathogenic biotrophic bacteria Xanthomonas campestris (e.g. pv. campestris (Xcc), pv. raphani, pv. armoriaceae and pv. incanae) by restricting bacterial spread to the vascular system from the infection site; X.campestris causes black rot disease in crops (PubMed:24068949, PubMed:26355215, PubMed:30948526). Seems to not have any kinase activity (PubMed:24068949).[1] [2] [3]
References
- ↑ Huard-Chauveau C, Perchepied L, Debieu M, Rivas S, Kroj T, Kars I, Bergelson J, Roux F, Roby D. An atypical kinase under balancing selection confers broad-spectrum disease resistance in Arabidopsis. PLoS Genet. 2013;9(9):e1003766. PMID:24068949 doi:10.1371/journal.pgen.1003766
- ↑ Wang G, Roux B, Feng F, Guy E, Li L, Li N, Zhang X, Lautier M, Jardinaud MF, Chabannes M, Arlat M, Chen S, He C, Noël LD, Zhou JM. The Decoy Substrate of a Pathogen Effector and a Pseudokinase Specify Pathogen-Induced Modified-Self Recognition and Immunity in Plants. Cell Host Microbe. 2015 Sep 9;18(3):285-95. PMID:26355215 doi:10.1016/j.chom.2015.08.004
- ↑ 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
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