4nfu

From Proteopedia

(Difference between revisions)

Revision as of 08:26, 11 January 2023

Structure of the central plant immunity signaling node EDS1 in complex with its interaction partner SAG101

Structural highlights

4nfu 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.
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EDS1L_ARATH Positive regulator of basal resistance and of effector-triggered immunity specifically mediated by TIR-NB-LRR resistance proteins. Disruption by bacterial effector of EDS1-TIR-NB-LRR resistance protein interactions constitutes the first step in resistance activation (PubMed:22158819). Triggers early plant defenses and hypersensitive response independently of PAD4, and then recruits PAD4 to potentiate plant defenses through the accumulation of salicylic acid (PubMed:11574472). Nuclear localization is essential for basal and TIR-NB-LRR-conditioned immunity and for reprogramming defense gene expression, while cytoplasmic EDS1 is required to induce a complete immune response (PubMed:20617163). Heterodimerization with PAD4 or SGA101 is necessary for TNL-mediated effector-triggered immunity (PubMed:24331460). Contributes to nonhost resistance against E.amylovora (PubMed:22316300). Has no direct lipase activity (PubMed:16040633).^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

Publication Abstract from PubMed

Biotrophic plant pathogens encounter a postinfection basal resistance layer controlled by the lipase-like protein enhanced disease susceptibility 1 (EDS1) and its sequence-related interaction partners, senescence-associated gene 101 (SAG101) and phytoalexin deficient 4 (PAD4). Maintainance of separate EDS1 family member clades through angiosperm evolution suggests distinct functional attributes. We report the Arabidopsis EDS1-SAG101 heterodimer crystal structure with juxtaposed N-terminal alpha/beta hydrolase and C-terminal alpha-helical EP domains aligned via a large conserved interface. Mutational analysis of the EDS1-SAG101 heterodimer and a derived EDS1-PAD4 structural model shows that EDS1 signals within mutually exclusive heterocomplexes. Although there is evolutionary conservation of alpha/beta hydrolase topology in all three proteins, a noncatalytic resistance mechanism is indicated. Instead, the respective N-terminal domains appear to facilitate binding of the essential EP domains to create novel interaction surfaces on the heterodimer. Transitions between distinct functional EDS1 heterodimers might explain the central importance and versatility of this regulatory node in plant immunity.

Structural basis for signaling by exclusive EDS1 heteromeric complexes with SAG101 or PAD4 in plant innate immunity.,Wagner S, Stuttmann J, Rietz S, Guerois R, Brunstein E, Bautor J, Niefind K, Parker JE Cell Host Microbe. 2013 Dec 11;14(6):619-30. doi: 10.1016/j.chom.2013.11.006. PMID:24331460^[8]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Falk A, Feys BJ, Frost LN, Jones JD, Daniels MJ, Parker JE. EDS1, an essential component of R gene-mediated disease resistance in Arabidopsis has homology to eukaryotic lipases. Proc Natl Acad Sci U S A. 1999 Mar 16;96(6):3292-7. doi: 10.1073/pnas.96.6.3292. PMID:10077677 doi:http://dx.doi.org/10.1073/pnas.96.6.3292
↑ Feys BJ, Moisan LJ, Newman MA, Parker JE. Direct interaction between the Arabidopsis disease resistance signaling proteins, EDS1 and PAD4. EMBO J. 2001 Oct 1;20(19):5400-11. doi: 10.1093/emboj/20.19.5400. PMID:11574472 doi:http://dx.doi.org/10.1093/emboj/20.19.5400
↑ Garcia AV, Blanvillain-Baufume S, Huibers RP, Wiermer M, Li G, Gobbato E, Rietz S, Parker JE. Balanced nuclear and cytoplasmic activities of EDS1 are required for a complete plant innate immune response. PLoS Pathog. 2010 Jul 1;6:e1000970. doi: 10.1371/journal.ppat.1000970. PMID:20617163 doi:http://dx.doi.org/10.1371/journal.ppat.1000970
↑ Bhattacharjee S, Halane MK, Kim SH, Gassmann W. Pathogen effectors target Arabidopsis EDS1 and alter its interactions with immune regulators. Science. 2011 Dec 9;334(6061):1405-8. doi: 10.1126/science.1211592. PMID:22158819 doi:http://dx.doi.org/10.1126/science.1211592
↑ Moreau M, Degrave A, Vedel R, Bitton F, Patrit O, Renou JP, Barny MA, Fagard M. EDS1 contributes to nonhost resistance of Arabidopsis thaliana against Erwinia amylovora. Mol Plant Microbe Interact. 2012 Mar;25(3):421-30. doi: 10.1094/MPMI-05-11-0111. PMID:22316300 doi:http://dx.doi.org/10.1094/MPMI-05-11-0111
↑ Wagner S, Stuttmann J, Rietz S, Guerois R, Brunstein E, Bautor J, Niefind K, Parker JE. Structural basis for signaling by exclusive EDS1 heteromeric complexes with SAG101 or PAD4 in plant innate immunity. Cell Host Microbe. 2013 Dec 11;14(6):619-30. doi: 10.1016/j.chom.2013.11.006. PMID:24331460 doi:http://dx.doi.org/10.1016/j.chom.2013.11.006
↑ Feys BJ, Wiermer M, Bhat RA, Moisan LJ, Medina-Escobar N, Neu C, Cabral A, Parker JE. Arabidopsis SENESCENCE-ASSOCIATED GENE101 stabilizes and signals within an ENHANCED DISEASE SUSCEPTIBILITY1 complex in plant innate immunity. Plant Cell. 2005 Sep;17(9):2601-13. Epub 2005 Jul 22. PMID:16040633 doi:http://dx.doi.org/tpc.105.033910
↑ Wagner S, Stuttmann J, Rietz S, Guerois R, Brunstein E, Bautor J, Niefind K, Parker JE. Structural basis for signaling by exclusive EDS1 heteromeric complexes with SAG101 or PAD4 in plant innate immunity. Cell Host Microbe. 2013 Dec 11;14(6):619-30. doi: 10.1016/j.chom.2013.11.006. PMID:24331460 doi:http://dx.doi.org/10.1016/j.chom.2013.11.006

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/4nfu"

@@ Line 1: / Line 1: @@
 ==Structure of the central plant immunity signaling node EDS1 in complex with its interaction partner SAG101==
-<StructureSection load='4nfu' size='340' side='right' caption='[[4nfu]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
+<StructureSection load='4nfu' size='340' side='right'caption='[[4nfu]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4nfu]] 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=4NFU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NFU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4nfu]] 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=4NFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NFU FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EDS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH]), At5g14930, F2G14.50, SAG101 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=4nfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nfu OCA], [https://pdbe.org/4nfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nfu RCSB], [https://www.ebi.ac.uk/pdbsum/4nfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nfu ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxylesterase Carboxylesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.1 3.1.1.1] </span></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=4nfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nfu OCA], [http://pdbe.org/4nfu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nfu RCSB], [http://www.ebi.ac.uk/pdbsum/4nfu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nfu ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SG101_ARATH SG101_ARATH]] Acyl hydrolase that triggers the leaf senescence onset. Can use triolein as substrate to produce oleic acids.<ref>PMID:11971136</ref> <ref>PMID:16040633</ref> <ref>PMID:22072959</ref> <ref>PMID:23356583</ref>   Involved in the EDS1-dependent intrinsic and indispensable resistance signaling pathway; together with PAD4, required for programmed cell death triggered by RPS4 in response to avirulent pathogens (e.g. Pseudomonas syringae pv. tomato strain DC3000 and Hyaloperonospora parasitica isolates CALA2 and EMWA1) and in restricting the growth of virulent pathogens (e.g. H. parasitica isolates NOCO2 and P.syringae pv. tomato strain DC3000 avrRps4). Regulates the nuclear localization of EDS1. Essential for the RPP8/HRT-mediated resistance to the turnip crinkle virus (TCV). Involved in the post-invasion resistance to Phakopsora pachyrhizi in the mesophyll.<ref>PMID:11971136</ref> <ref>PMID:16040633</ref> <ref>PMID:22072959</ref> <ref>PMID:23356583</ref>
+[https://www.uniprot.org/uniprot/EDS1L_ARATH EDS1L_ARATH] Positive regulator of basal resistance and of effector-triggered immunity specifically mediated by TIR-NB-LRR resistance proteins. Disruption by bacterial effector of EDS1-TIR-NB-LRR resistance protein interactions constitutes the first step in resistance activation (PubMed:22158819). Triggers early plant defenses and hypersensitive response independently of PAD4, and then recruits PAD4 to potentiate plant defenses through the accumulation of salicylic acid (PubMed:11574472). Nuclear localization is essential for basal and TIR-NB-LRR-conditioned immunity and for reprogramming defense gene expression, while cytoplasmic EDS1 is required to induce a complete immune response (PubMed:20617163). Heterodimerization with PAD4 or SGA101 is necessary for TNL-mediated effector-triggered immunity (PubMed:24331460). Contributes to nonhost resistance against E.amylovora (PubMed:22316300). Has no direct lipase activity (PubMed:16040633).<ref>PMID:10077677</ref> <ref>PMID:11574472</ref> <ref>PMID:20617163</ref> <ref>PMID:22158819</ref> <ref>PMID:22316300</ref> <ref>PMID:24331460</ref> <ref>PMID:16040633</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Arath]]
+[[Category: Arabidopsis thaliana]]
-[[Category: Carboxylesterase]]
+[[Category: Large Structures]]
-[[Category: Guerois, R]]
+[[Category: Guerois R]]
-[[Category: Niefind, K]]
+[[Category: Niefind K]]
-[[Category: Parker, J E]]
+[[Category: Parker JE]]
-[[Category: Rietz, S]]
+[[Category: Rietz S]]
-[[Category: Stuttmann, J]]
+[[Category: Stuttmann J]]
-[[Category: Wagner, S]]
+[[Category: Wagner S]]
-[[Category: Alpha/beta hydrolase fold]]
-[[Category: Hydrolase]]
-[[Category: Innate immunity]]
-[[Category: Nucleus]]
-[[Category: Pad4]]
-[[Category: Pathogen defense]]
-[[Category: Phytoalexin deficient 4]]
-[[Category: Signaling protein]]

4nfu

From Proteopedia

Revision as of 08:26, 11 January 2023

Structure of the central plant immunity signaling node EDS1 in complex with its interaction partner SAG101

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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