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5HYX

Plant peptide hormone receptor RGFR1 in complex with RGF1

Summary for 5HYX
Entry DOI10.2210/pdb5hyx/pdb
Related5HZ0 5HZ1 5HZ3
DescriptorProbable LRR receptor-like serine/threonine-protein kinase At4g26540, PTR-SER-ASN-PRO-GLY-HIS-HIS-PRO-HYP-ARG-HIS-ASN, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
Functional Keywordsplant receptor, transferase
Biological sourceArabidopsis thaliana (Mouse-ear cress)
More
Total number of polymer chains2
Total formula weight71697.26
Authors
Song, W.,Han, Z.,Chai, J. (deposition date: 2016-02-02, release date: 2017-01-11, Last modification date: 2025-04-09)
Primary citationSong, W.,Liu, L.,Wang, J.,Wu, Z.,Zhang, H.,Tang, J.,Lin, G.,Wang, Y.,Wen, X.,Li, W.,Han, Z.,Guo, H.,Chai, J.
Signature motif-guided identification of receptors for peptide hormones essential for root meristem growth
Cell Res., 26:674-685, 2016
Cited by
PubMed Abstract: Peptide-mediated cell-to-cell signaling has crucial roles in coordination and definition of cellular functions in plants. Peptide-receptor matching is important for understanding the mechanisms underlying peptide-mediated signaling. Here we report the structure-guided identification of root meristem growth factor (RGF) receptors important for plant development. An assay based on a signature ligand recognition motif (Arg-x-Arg) conserved in a subfamily of leucine-rich repeat receptor kinases (LRR-RKs) identified the functionally uncharacterized LRR-RK At4g26540 as a receptor of RGF1 (RGFR1). We further solved the crystal structure of RGF1 in complex with the LRR domain of RGFR1 at a resolution of 2.6 Å, which reveals that the Arg-x-Gly-Gly (RxGG) motif is responsible for specific recognition of the sulfate group of RGF1 by RGFR1. Based on the RxGG motif, we identified additional four RGFRs. Participation of the five RGFRs in RGF-induced signaling is supported by biochemical and genetic data. We also offer evidence showing that SERKs function as co-receptors for RGFs. Taken together, our study identifies RGF receptors and co-receptors that can link RGF signals with their downstream components and provides a proof of principle for structure-based matching of LRR-RKs with their peptide ligands.
PubMed: 27229311
DOI: 10.1038/cr.2016.62
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.596 Å)
Structure validation

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