6i8h

From Proteopedia

(Difference between revisions)

Revision as of 11:32, 13 November 2019

Structure of the plant immune signaling node EDS1 (enhanced disease susceptibility 1) in complex with nanobody ENB15

Structural highlights

6i8h is a 2 chain structure with sequence from Arath and Camelus glama. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	EDS1 (ARATH)
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

In plant innate immunity, enhanced disease susceptibility 1 (EDS1) integrates all pathogen-induced signals transmitted by TIR-type NLR receptors. Driven by an N-terminal alpha/beta-hydrolase-folded domain with a protruding interaction helix, EDS1 assembles with two homologs, phytoalexin-deficient 4 (PAD4) and senescence-associated gene 101 (SAG101). The resulting heterodimers are critical for EDS1 function and structurally well characterized. Here, we resolve solution and crystal structures of unbound Arabidopsis thaliana EDS1 (AtEDS1) using nanobodies for crystallization. These structures, together with gel filtration and immunoprecipitation data, show that PAD4/SAG101-unbound AtEDS1 is stable as a monomer and does not form the homodimers recorded in public databases. Its PAD4/SAG101 anchoring helix is disordered unless engaged in protein/protein interactions. As in the complex with SAG101, monomeric AtEDS1 has a substrate-inaccessible esterase triad with a blocked oxyanion hole and without space for a covalent acyl intermediate. These new structures suggest that the AtEDS1 monomer represents an inactive or pre-activated ground state.

Arabidopsis immunity regulator EDS1 in a PAD4/SAG101-unbound form is a monomer with an inherently inactive conformation.,Voss M, Toelzer C, Bhandari DD, Parker JE, Niefind K J Struct Biol. 2019 Sep 21. pii: S1047-8477(19)30201-1. doi:, 10.1016/j.jsb.2019.09.007. PMID:31550533^[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
↑ Voss M, Toelzer C, Bhandari DD, Parker JE, Niefind K. Arabidopsis immunity regulator EDS1 in a PAD4/SAG101-unbound form is a monomer with an inherently inactive conformation. J Struct Biol. 2019 Sep 21. pii: S1047-8477(19)30201-1. doi:, 10.1016/j.jsb.2019.09.007. PMID:31550533 doi:http://dx.doi.org/10.1016/j.jsb.2019.09.007

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/6i8h"

@@ Line 3: / Line 3: @@
 <StructureSection load='6i8h' size='340' side='right'caption='[[6i8h]], [[Resolution|resolution]] 3.68&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6i8h]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I8H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I8H FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6i8h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath] and [http://en.wikipedia.org/wiki/Camelus_glama Camelus glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I8H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I8H FirstGlance]. <br>
-</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=6i8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i8h OCA], [http://pdbe.org/6i8h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i8h RCSB], [http://www.ebi.ac.uk/pdbsum/6i8h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i8h ProSAT]</span></td></tr>
+</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])</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=6i8h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i8h OCA], [http://pdbe.org/6i8h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i8h RCSB], [http://www.ebi.ac.uk/pdbsum/6i8h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i8h ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Arath]]
+[[Category: Camelus glama]]
 [[Category: Large Structures]]
 [[Category: Niefind, K]]

6i8h

From Proteopedia

Revision as of 11:32, 13 November 2019

Structure of the plant immune signaling node EDS1 (enhanced disease susceptibility 1) in complex with nanobody ENB15

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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