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| | ==Crystal structure of the TIR domain from the Arabidopsis thaliana NLR protein SNC1== | | ==Crystal structure of the TIR domain from the Arabidopsis thaliana NLR protein SNC1== |
| - | <StructureSection load='5tec' size='340' side='right' caption='[[5tec]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='5tec' size='340' side='right'caption='[[5tec]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5tec]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TEC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5tec]] 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=5TEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TEC FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5teb|5teb]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tec OCA], [http://pdbe.org/5tec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tec RCSB], [http://www.ebi.ac.uk/pdbsum/5tec PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tec 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=5tec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tec OCA], [https://pdbe.org/5tec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tec RCSB], [https://www.ebi.ac.uk/pdbsum/5tec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tec ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SNC1_ARATH SNC1_ARATH]] Disease resistance protein of the TIR-NB-LRR-type. Part of the RPP5 locus that contains a cluster of several paralogous disease resistance (R) genes. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth. Regulated by RNA silencing. Expression regulated by MOS1 at chromatin level. Negatively regulated at the transcript level by BON1. Nuclear localization of SNC1 is essential for its activity (PubMed:22454454). ABA deficiency can rescue high-temperature inhibition of SNC1-mediated defense responses (PubMed:22454454).<ref>PMID:14576290</ref> <ref>PMID:20647385</ref> <ref>PMID:22454454</ref> | + | [https://www.uniprot.org/uniprot/SNC1_ARATH SNC1_ARATH] Disease resistance protein of the TIR-NB-LRR-type. Part of the RPP5 locus that contains a cluster of several paralogous disease resistance (R) genes. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth. Regulated by RNA silencing. Expression regulated by MOS1 at chromatin level. Negatively regulated at the transcript level by BON1. Nuclear localization of SNC1 is essential for its activity (PubMed:22454454). ABA deficiency can rescue high-temperature inhibition of SNC1-mediated defense responses (PubMed:22454454).<ref>PMID:14576290</ref> <ref>PMID:20647385</ref> <ref>PMID:22454454</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| - | The Toll/interleukin-1 receptor (TIR) domain is a protein-protein interaction domain that is found in both animal and plant immune receptors. The N-terminal TIR domain from the nucleotide-binding (NB)-leucine-rich repeat (LRR) class of plant disease-resistance (R) proteins has been shown to play an important role in defence signalling. Recently, the crystal structure of the TIR domain from flax R protein L6 was determined and this structure, combined with functional studies, demonstrated that TIR-domain homodimerization is a requirement for function of the R protein L6. To advance the molecular understanding of the function of TIR domains in R-protein signalling, the protein expression, purification, crystallization and X-ray diffraction analyses of the TIR domains of the Arabidopsis thaliana R proteins RPS4 (resistance to Pseudomonas syringae 4) and RRS1 (resistance to Ralstonia solanacearum 1) and the resistance-like protein SNC1 (suppressor of npr1-1, constitutive 1) are reported here. RPS4 and RRS1 function cooperatively as a dual resistance-protein system that prevents infection by three distinct pathogens. SNC1 is implicated in resistance pathways in Arabidopsis and is believed to be involved in transcriptional regulation through its interaction with the transcriptional corepressor TPR1 (Topless-related 1). The TIR domains of all three proteins have successfully been expressed and purified as soluble proteins in Escherichia coli. Plate-like crystals of the RPS4 TIR domain were obtained using PEG 3350 as a precipitant; they diffracted X-rays to 2.05 A resolution, had the symmetry of space group P1 and analysis of the Matthews coefficient suggested that there were four molecules per asymmetric unit. Tetragonal crystals of the RRS1 TIR domain were obtained using ammonium sulfate as a precipitant; they diffracted X-rays to 1.75 A resolution, had the symmetry of space group P4(1)2(1)2 or P4(3)2(1)2 and were most likely to contain one molecule per asymmetric unit. Crystals of the SNC1 TIR domain were obtained using PEG 3350 as a precipitant; they diffracted X-rays to 2.20 A resolution and had the symmetry of space group P4(1)2(1)2 or P4(3)2(1)2, with two molecules predicted per asymmetric unit. These results provide a good foundation to advance the molecular and structural understanding of the function of the TIR domain in plant innate immunity. | + | The self-association of Toll/interleukin-1 receptor/resistance protein (TIR) domains has been implicated in signaling in plant and animal immunity receptors. Structure-based studies identified different TIR-domain dimerization interfaces required for signaling of the plant nucleotide-binding oligomerization domain-like receptors (NLRs) L6 from flax and disease resistance protein RPS4 from Arabidopsis Here we show that the crystal structure of the TIR domain from the Arabidopsis NLR suppressor of npr1-1, constitutive 1 (SNC1) contains both an L6-like interface involving helices alphaD and alphaE (DE interface) and an RPS4-like interface involving helices alphaA and alphaE (AE interface). Mutations in either the AE- or DE-interface region disrupt cell-death signaling activity of SNC1, L6, and RPS4 TIR domains and full-length L6 and RPS4. Self-association of L6 and RPS4 TIR domains is affected by mutations in either region, whereas only AE-interface mutations affect SNC1 TIR-domain self-association. We further show two similar interfaces in the crystal structure of the TIR domain from the Arabidopsis NLR recognition of Peronospora parasitica 1 (RPP1). These data demonstrate that both the AE and DE self-association interfaces are simultaneously required for self-association and cell-death signaling in diverse plant NLRs. |
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| - | Crystallization and preliminary X-ray diffraction analyses of the TIR domains of three TIR-NB-LRR proteins that are involved in disease resistance in Arabidopsis thaliana.,Wan L, Zhang X, Williams SJ, Ve T, Bernoux M, Sohn KH, Jones JD, Dodds PN, Kobe B Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Nov;69(Pt 11):1275-80., doi: 10.1107/S1744309113026614. Epub 2013 Oct 30. PMID:24192368<ref>PMID:24192368</ref>
| + | Multiple functional self-association interfaces in plant TIR domains.,Zhang X, Bernoux M, Bentham AR, Newman TE, Ve T, Casey LW, Raaymakers TM, Hu J, Croll TI, Schreiber KJ, Staskawicz BJ, Anderson PA, Sohn KH, Williams SJ, Dodds PN, Kobe B Proc Natl Acad Sci U S A. 2017 Feb 3. pii: 201621248. doi:, 10.1073/pnas.1621248114. PMID:28159890<ref>PMID:28159890</ref> |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bentham, A]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Kobe, B]] | + | [[Category: Large Structures]] |
| - | [[Category: Ve, T]] | + | [[Category: Bentham A]] |
| - | [[Category: Williams, S J]] | + | [[Category: Kobe B]] |
| - | [[Category: Zhang, X]] | + | [[Category: Ve T]] |
| - | [[Category: Immune system]] | + | [[Category: Williams SJ]] |
| - | [[Category: Plant nlr]] | + | [[Category: Zhang X]] |
| - | [[Category: Tir domain]]
| + | |
| Structural highlights
Function
SNC1_ARATH Disease resistance protein of the TIR-NB-LRR-type. Part of the RPP5 locus that contains a cluster of several paralogous disease resistance (R) genes. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth. Regulated by RNA silencing. Expression regulated by MOS1 at chromatin level. Negatively regulated at the transcript level by BON1. Nuclear localization of SNC1 is essential for its activity (PubMed:22454454). ABA deficiency can rescue high-temperature inhibition of SNC1-mediated defense responses (PubMed:22454454).[1] [2] [3]
Publication Abstract from PubMed
The self-association of Toll/interleukin-1 receptor/resistance protein (TIR) domains has been implicated in signaling in plant and animal immunity receptors. Structure-based studies identified different TIR-domain dimerization interfaces required for signaling of the plant nucleotide-binding oligomerization domain-like receptors (NLRs) L6 from flax and disease resistance protein RPS4 from Arabidopsis Here we show that the crystal structure of the TIR domain from the Arabidopsis NLR suppressor of npr1-1, constitutive 1 (SNC1) contains both an L6-like interface involving helices alphaD and alphaE (DE interface) and an RPS4-like interface involving helices alphaA and alphaE (AE interface). Mutations in either the AE- or DE-interface region disrupt cell-death signaling activity of SNC1, L6, and RPS4 TIR domains and full-length L6 and RPS4. Self-association of L6 and RPS4 TIR domains is affected by mutations in either region, whereas only AE-interface mutations affect SNC1 TIR-domain self-association. We further show two similar interfaces in the crystal structure of the TIR domain from the Arabidopsis NLR recognition of Peronospora parasitica 1 (RPP1). These data demonstrate that both the AE and DE self-association interfaces are simultaneously required for self-association and cell-death signaling in diverse plant NLRs.
Multiple functional self-association interfaces in plant TIR domains.,Zhang X, Bernoux M, Bentham AR, Newman TE, Ve T, Casey LW, Raaymakers TM, Hu J, Croll TI, Schreiber KJ, Staskawicz BJ, Anderson PA, Sohn KH, Williams SJ, Dodds PN, Kobe B Proc Natl Acad Sci U S A. 2017 Feb 3. pii: 201621248. doi:, 10.1073/pnas.1621248114. PMID:28159890[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang Y, Goritschnig S, Dong X, Li X. A gain-of-function mutation in a plant disease resistance gene leads to constitutive activation of downstream signal transduction pathways in suppressor of npr1-1, constitutive 1. Plant Cell. 2003 Nov;15(11):2636-46. Epub 2003 Oct 23. PMID:14576290 doi:http://dx.doi.org/10.1105/tpc.015842
- ↑ Zhu Z, Xu F, Zhang Y, Cheng YT, Wiermer M, Li X, Zhang Y. Arabidopsis resistance protein SNC1 activates immune responses through association with a transcriptional corepressor. Proc Natl Acad Sci U S A. 2010 Aug 3;107(31):13960-5. doi:, 10.1073/pnas.1002828107. Epub 2010 Jul 20. PMID:20647385 doi:http://dx.doi.org/10.1073/pnas.1002828107
- ↑ Mang HG, Qian W, Zhu Y, Qian J, Kang HG, Klessig DF, Hua J. Abscisic acid deficiency antagonizes high-temperature inhibition of disease resistance through enhancing nuclear accumulation of resistance proteins SNC1 and RPS4 in Arabidopsis. Plant Cell. 2012 Mar;24(3):1271-84. doi: 10.1105/tpc.112.096198. Epub 2012 Mar, 27. PMID:22454454 doi:http://dx.doi.org/10.1105/tpc.112.096198
- ↑ Zhang X, Bernoux M, Bentham AR, Newman TE, Ve T, Casey LW, Raaymakers TM, Hu J, Croll TI, Schreiber KJ, Staskawicz BJ, Anderson PA, Sohn KH, Williams SJ, Dodds PN, Kobe B. Multiple functional self-association interfaces in plant TIR domains. Proc Natl Acad Sci U S A. 2017 Feb 3. pii: 201621248. doi:, 10.1073/pnas.1621248114. PMID:28159890 doi:http://dx.doi.org/10.1073/pnas.1621248114
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