6QUP

Structural signatures in EPR3 define a unique class of plant carbohydrate receptors

6QUP の概要

• エントリーDOI: 10.2210/pdb6qup/pdb
• 分子名称: LysM type receptor kinase, Nanobody 186 (Nb186), 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: lysm protein, plant protein, nitrogen fixation, plant receptor
• 由来する生物種: Lotus japonicus; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37931.91

構造登録者

Wong, J.E.,Gysel, K.,Birkefeldt, T.G.,Vinther, M.,Muszynski, A.,Azadi, P.,Laursen, N.S.,Sullivan, J.T.,Ronson, C.W.,Stougaard, J.,Andersen, K.R. (登録日: 2019-02-28, 公開日: 2020-08-05, 最終更新日: 2024-11-13)

主引用文献

Wong, J.E.M.M.,Gysel, K.,Birkefeldt, T.G.,Vinther, M.,Muszynski, A.,Azadi, P.,Laursen, N.S.,Sullivan, J.T.,Ronson, C.W.,Stougaard, J.,Andersen, K.R.
Structural signatures in EPR3 define a unique class of plant carbohydrate receptors.
Nat Commun, 11:3797-3797, 2020

PubMed Abstract: Receptor-mediated perception of surface-exposed carbohydrates like lipo- and exo-polysaccharides (EPS) is important for non-self recognition and responses to microbial associated molecular patterns in mammals and plants. In legumes, EPS are monitored and can either block or promote symbiosis with rhizobia depending on their molecular composition. To establish a deeper understanding of receptors involved in EPS recognition, we determined the structure of the Lotus japonicus (Lotus) exopolysaccharide receptor 3 (EPR3) ectodomain. EPR3 forms a compact structure built of three putative carbohydrate-binding modules (M1, M2 and LysM3). M1 and M2 have unique βαββ and βαβ folds that have not previously been observed in carbohydrate binding proteins, while LysM3 has a canonical βααβ fold. We demonstrate that this configuration is a structural signature for a ubiquitous class of receptors in the plant kingdom. We show that EPR3 is promiscuous, suggesting that plants can monitor complex microbial communities though this class of receptors.

PubMed: 32732998
DOI: 10.1038/s41467-020-17568-9

実験手法

X-RAY DIFFRACTION (1.871 Å)