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4NFU

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

4NFU の概要
エントリーDOI10.2210/pdb4nfu/pdb
分子名称EDS1, Senescence-associated carboxylesterase 101, beta-D-glucopyranose, ... (6 entities in total)
機能のキーワードalpha/beta hydrolase fold, innate immunity, pathogen defense, phytoalexin deficient 4, pad4, nucleus, hydrolase, signaling protein
由来する生物種Arabidopsis thaliana (mouse-ear cress)
詳細
細胞内の位置Membrane; Single-pass membrane protein (Potential): Q4F883
タンパク質・核酸の鎖数2
化学式量合計136200.93
構造登録者
Wagner, S.,Stuttmann, J.,Rietz, S.,Guerois, R.,Niefind, K.,Parker, J.E. (登録日: 2013-11-01, 公開日: 2013-12-11, 最終更新日: 2024-02-28)
主引用文献Wagner, S.,Stuttmann, J.,Rietz, S.,Guerois, R.,Brunstein, E.,Bautor, J.,Niefind, K.,Parker, J.E.
Structural Basis for Signaling by Exclusive EDS1 Heteromeric Complexes with SAG101 or PAD4 in Plant Innate Immunity.
Cell Host Microbe, 14:619-630, 2013
Cited by
PubMed Abstract: 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 α/β hydrolase and C-terminal α-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 α/β 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.
PubMed: 24331460
DOI: 10.1016/j.chom.2013.11.006
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.21 Å)
構造検証レポート
Validation report summary of 4nfu
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-20に公開中

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