4nfu

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== Structural highlights ==
== Structural highlights ==
<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>
<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21&#8491;</td></tr>
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<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='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='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>
</table>
</table>
== Function ==
== Function ==
[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>
[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>
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== Publication Abstract from PubMed ==
 
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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.
 
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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<ref>PMID:24331460</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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<div class="pdbe-citations 4nfu" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
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<references/>

Current revision

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

PDB ID 4nfu

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