Universität zu Köln

Voss, Martin, Toelzer, Christine, Bhandari, Deepak D., Parker, Jane E. and Niefind, Karsten ORCID: 0000-0002-0183-6315 (2019). Arabidopsis immunity regulator EDS1 in a PAD4/SAG101-unbound form is a monomer with an inherently inactive conformation. J. Struct. Biol., 208 (3). SAN DIEGO: ACADEMIC PRESS INC ELSEVIER SCIENCE. ISSN 1095-8657

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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 alpha/beta-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.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Voss, Martin UNSPECIFIED UNSPECIFIED UNSPECIFIED Toelzer, Christine UNSPECIFIED UNSPECIFIED UNSPECIFIED Bhandari, Deepak D. UNSPECIFIED UNSPECIFIED UNSPECIFIED Parker, Jane E. UNSPECIFIED UNSPECIFIED UNSPECIFIED Niefind, Karsten UNSPECIFIED orcid.org/0000-0002-0183-6315 UNSPECIFIED
URN:	urn:nbn:de:hbz:38-126101
DOI:	10.1016/j.jsb.2019.09.007
Journal or Publication Title:	J. Struct. Biol.
Volume:	208
Number:	3
Date:	2019
Publisher:	ACADEMIC PRESS INC ELSEVIER SCIENCE
Place of Publication:	SAN DIEGO
ISSN:	1095-8657
Language:	English
Faculty:	Faculty of Mathematics and Natural Sciences
Divisions:	Faculty of Mathematics and Natural Sciences > Department of Chemistry > Institute of Biochemistry
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language SMALL-ANGLE SCATTERING; SALICYLIC-ACID; BIOLOGICAL MACROMOLECULES; DISEASE RESISTANCE; CELL-DEATH; PROTEIN; PAD4; HYDROLASE; SENESCENCE; DEFENSE Multiple languages Biochemistry & Molecular Biology; Biophysics; Cell Biology Multiple languages
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/12610