Arabidopsis immunity regulator EDS1 in a PAD4/SAG101-unbound form is a monomer with an inherently inactive conformation

Martin Voss, Christine Toelzer, Deepak D. Bhandari, Jane E. Parker, Karsten Niefind*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)

4 Citations (Scopus)

Abstract

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 α/β-hydrolase-fold 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.

Original languageEnglish
Article number107390
JournalJournal of Structural Biology
Volume208
Issue number3
Early online date21 Sep 2019
DOIs
Publication statusPublished - 1 Dec 2019

Structured keywords

  • BrisSynBio
  • Bristol BioDesign Institute

Keywords

  • Enhanced disease susceptibility 1 (EDS1)
  • Nanobody
  • Plant innate immunity
  • Pseudo-enzyme
  • Senescence-associated gene 101 (SAG101)
  • α/β-Hydrolase fold
  • Synthetic biology

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