5tec

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the TIR domain from the Arabidopsis thaliana NLR protein SNC1

Structural highlights

5tec is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5tec"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the TIR domain from the Arabidopsis thaliana NLR protein SNC1==
-<StructureSection load='5tec' size='340' side='right' caption='[[5tec]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='5tec' size='340' side='right'caption='[[5tec]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == 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]] 2.2&#8491;</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>
 == 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;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 __TOC__
 </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]]

5tec

From Proteopedia

Current revision

Crystal structure of the TIR domain from the Arabidopsis thaliana NLR protein SNC1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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