8B28

Structure of an intron-retention variant of the plant immune signalling protein EDS1 from Vitis vinifera

8B28 の概要

• エントリーDOI: 10.2210/pdb8b28/pdb
• 分子名称: Enhanced disease susceptibility 1, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: enhanced disease susceptibility 1 plant innate immune system intron retention during alternative splicing, immune system
• 由来する生物種: Vitis vinifera (wine grape)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44145.10

構造登録者

Voss, M.,Niefind, K. (登録日: 2022-09-13, 公開日: 2023-04-05, 最終更新日: 2024-02-07)

主引用文献

Voss, M.,Cseke, L.J.,Gassmann, W.,Niefind, K.
A splicing variant of EDS1 from Vitis vinifera forms homodimers but no heterodimers with PAD4.
Protein Sci., 32:e4624-e4624, 2023

PubMed Abstract: Enhanced Disease Susceptibility 1 (EDS1), a key component of microbe-triggered immunity and effector-triggered immunity in most higher plants, forms functional heterodimeric complexes with its homologs Phytoalexin Deficient 4 (PAD4) or Senescence-associated Gene 101 (SAG101). Here, the crystal structure of VvEDS1 , the N-terminal domain of EDS1 from Vitis vinifera, is reported, representing the first structure of an EDS1 entity beyond the model plant Arabidopsis thaliana. VvEDS1 has an α/β-hydrolase fold, is similar to the N-terminal domain of A. thaliana EDS1 and forms stable homodimers in solution as well as in crystals. These VvEDS1 homodimers are spatially incompatible with heterodimers with PAD4 or SAG101, they explain why VvEDS1 does not interact with V. vinifera PAD4 according to gel filtration, and they serve as a guide to develop a plausible, albeit experimentally not verified model of full-length EDS1. VvEDS1 is a splicing variant comprising two of three exons of the VvEDS1 gene. It originates from a naturally occurring mRNA, in which the first of two introns was removed while the second one containing a stop codon close to the exon/intron border was retained. This is a potential case of intron retention and the first report of this phenomenon in the context of EDS1. Its biological significance has not yet been clarified, nor has the question if a VvEDS1 protein with a specific function can occur under physiological conditions.

PubMed: 36917448
DOI: 10.1002/pro.4624

実験手法

X-RAY DIFFRACTION (1.75 Å)