6r85 | pdb_00006r85

Structure of Arabidopsis thaliana GLR3.3 ligand-binding domain in complex with L-glutamate

spinqualitylabelsall models 6r85, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6r85 is a 2 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, GLU, NA, SO4 Gene: GLR3.3, At1g42540, T8D8.1 (ARATH) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GLR33_ARATH] Glutamate-gated receptor that probably acts as non-selective cation channel, at least in roots and hypocotyls. Can be triggered by Ala, Asn, Cys, Glu, Gly, Ser and glutathione (a tripeptide consisting of Glu-Gly-Cys). Mediates leaf-to-leaf wound signaling. May be involved in light-signal transduction and calcium homeostasis via the regulation of calcium influx into cells. Publication Abstract from PubMed Arabidopsis thaliana glutamate receptor-like (GLR) channels are amino acid-gated ion channels involved in physiological processes including wound signaling, stomatal regulation, and pollen tube growth. Here, fluorescence microscopy and genetics were used to confirm the central role of GLR3.3 in the amino acid-elicited cytosolic Ca(2+) increase in Arabidopsis seedling roots. To elucidate the binding properties of the receptor, we biochemically reconstituted the GLR3.3 ligand-binding domain (LBD) and analyzed its selectivity profile; our binding experiments revealed the LBD preference for l-Glu but also for sulfur-containing amino acids. Furthermore, we solved the crystal structures of the GLR3.3 LBD in complex with 4 different amino acid ligands, providing a rationale for how the LBD binding site evolved to accommodate diverse amino acids, thus laying the grounds for rational mutagenesis. Last, we inspected the structures of LBDs from nonplant species and generated homology models for other GLR isoforms. Our results establish that GLR3.3 is a receptor endowed with a unique amino acid ligand profile and provide a structural framework for engineering this and other GLR isoforms to investigate their physiology. The structural bases for agonist diversity in an Arabidopsis thaliana glutamate receptor-like channel.,Alfieri A, Doccula FG, Pederzoli R, Grenzi M, Bonza MC, Luoni L, Candeo A, Romano Armada N, Barbiroli A, Valentini G, Schneider TR, Bassi A, Bolognesi M, Nardini M, Costa A Proc Natl Acad Sci U S A. 2019 Dec 23. pii: 1905142117. doi:, 10.1073/pnas.1905142117. PMID:31871183 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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