4nfu | pdb_00004nfu

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

spinqualitylabelsall models 4nfu, resolution 2.21Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4nfu is a 2 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BGC, EPE, IPA Gene: EDS1 (ARATH), At5g14930, F2G14.50, SAG101 (ARATH) Activity: Carboxylesterase, with EC number 3.1.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SG101_ARATH] Acyl hydrolase that triggers the leaf senescence onset. Can use triolein as substrate to produce oleic acids. 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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