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| | <StructureSection load='7jlv' size='340' side='right'caption='[[7jlv]], [[Resolution|resolution]] 3.80Å' scene=''> | | <StructureSection load='7jlv' size='340' side='right'caption='[[7jlv]], [[Resolution|resolution]] 3.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7jlv]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Nicbe Nicbe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JLV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7JLV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7jlv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Nicotiana_benthamiana Nicotiana benthamiana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JLV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JLV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 3.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ROQ1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4100 NICBE])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ADP-ribosyl_cyclase/cyclic_ADP-ribose_hydrolase ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.6 3.2.2.6] </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=7jlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jlv OCA], [https://pdbe.org/7jlv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jlv RCSB], [https://www.ebi.ac.uk/pdbsum/7jlv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jlv ProSAT]</span></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=7jlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jlv OCA], [http://pdbe.org/7jlv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7jlv RCSB], [http://www.ebi.ac.uk/pdbsum/7jlv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7jlv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ROQ1_NICBE ROQ1_NICBE]] Disease resistance (R) protein that specifically recognizes the Xanthomonas and Pseudomonas effector proteins XopQ and HopQ1, and triggers cell death (PubMed:28891100). Acts as a NAD(+) hydrolase (NADase): in response to activation, catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide; NAD(+) cleavage triggering a defense system that promotes cell death (PubMed:31439792).<ref>PMID:28891100</ref> <ref>PMID:31439792</ref> | + | [https://www.uniprot.org/uniprot/ROQ1_NICBE ROQ1_NICBE] Disease resistance (R) protein that specifically recognizes the Xanthomonas and Pseudomonas effector proteins XopQ and HopQ1, and triggers cell death (PubMed:28891100). Acts as a NAD(+) hydrolase (NADase): in response to activation, catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide; NAD(+) cleavage triggering a defense system that promotes cell death (PubMed:31439792).<ref>PMID:28891100</ref> <ref>PMID:31439792</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Plants and animals detect pathogen infection using intracellular nucleotide-binding leucine-rich repeat receptors (NLRs) that directly or indirectly recognize pathogen effectors and activate an immune response. How effector sensing triggers NLR activation remains poorly understood. Here we describe the 3.8-angstrom-resolution cryo-electron microscopy structure of the activated ROQ1 (recognition of XopQ 1), an NLR native to Nicotiana benthamiana with a Toll-like interleukin-1 receptor (TIR) domain bound to the Xanthomonas euvesicatoria effector XopQ (Xanthomonas outer protein Q). ROQ1 directly binds to both the predicted active site and surface residues of XopQ while forming a tetrameric resistosome that brings together the TIR domains for downstream immune signaling. Our results suggest a mechanism for the direct recognition of effectors by NLRs leading to the oligomerization-dependent activation of a plant resistosome and signaling by the TIR domain.
| + | |
| - | | + | |
| - | Structure of the activated ROQ1 resistosome directly recognizing the pathogen effector XopQ.,Martin R, Qi T, Zhang H, Liu F, King M, Toth C, Nogales E, Staskawicz BJ Science. 2020 Dec 4;370(6521). pii: 370/6521/eabd9993. doi:, 10.1126/science.abd9993. PMID:33273074<ref>PMID:33273074</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 7jlv" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nicbe]] | + | [[Category: Nicotiana benthamiana]] |
| - | [[Category: King, M]] | + | [[Category: King M]] |
| - | [[Category: Lui, F]] | + | [[Category: Lui F]] |
| - | [[Category: Martin, R]] | + | [[Category: Martin R]] |
| - | [[Category: Nogales, E]] | + | [[Category: Nogales E]] |
| - | [[Category: Qi, T]] | + | [[Category: Qi T]] |
| - | [[Category: Staskawicz, B J]] | + | [[Category: Staskawicz BJ]] |
| - | [[Category: Toth, C]] | + | [[Category: Toth C]] |
| - | [[Category: Zhang, H]] | + | [[Category: Zhang H]] |
| - | [[Category: Effector]]
| + | |
| - | [[Category: Immune system]]
| + | |
| - | [[Category: Lrr]]
| + | |
| - | [[Category: Nb-arc]]
| + | |
| - | [[Category: Plant immunity]]
| + | |
| - | [[Category: Resistosome]]
| + | |
| - | [[Category: Tir]]
| + | |
| Structural highlights
Function
ROQ1_NICBE Disease resistance (R) protein that specifically recognizes the Xanthomonas and Pseudomonas effector proteins XopQ and HopQ1, and triggers cell death (PubMed:28891100). Acts as a NAD(+) hydrolase (NADase): in response to activation, catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide; NAD(+) cleavage triggering a defense system that promotes cell death (PubMed:31439792).[1] [2]
References
- ↑ Schultink A, Qi T, Lee A, Steinbrenner AD, Staskawicz B. Roq1 mediates recognition of the Xanthomonas and Pseudomonas effector proteins XopQ and HopQ1. Plant J. 2017 Dec;92(5):787-795. doi: 10.1111/tpj.13715. Epub 2017 Oct 25. PMID:28891100 doi:http://dx.doi.org/10.1111/tpj.13715
- ↑ Horsefield S, Burdett H, Zhang X, Manik MK, Shi Y, Chen J, Qi T, Gilley J, Lai JS, Rank MX, Casey LW, Gu W, Ericsson DJ, Foley G, Hughes RO, Bosanac T, von Itzstein M, Rathjen JP, Nanson JD, Boden M, Dry IB, Williams SJ, Staskawicz BJ, Coleman MP, Ve T, Dodds PN, Kobe B. NAD(+) cleavage activity by animal and plant TIR domains in cell death pathways. Science. 2019 Aug 23;365(6455):793-799. doi: 10.1126/science.aax1911. PMID:31439792 doi:http://dx.doi.org/10.1126/science.aax1911
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