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6QUP

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

Summary for 6QUP
Entry DOI10.2210/pdb6qup/pdb
DescriptorLysM type receptor kinase, Nanobody 186 (Nb186), 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
Functional Keywordslysm protein, plant protein, nitrogen fixation, plant receptor
Biological sourceLotus japonicus
More
Total number of polymer chains2
Total formula weight37931.91
Authors
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. (deposition date: 2019-02-28, release date: 2020-08-05, Last modification date: 2024-11-13)
Primary citationWong, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.871 Å)
Structure validation

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