6R8A
Structure of Arabidopsis thaliana GLR3.3 ligand-binding domain in complex with L-methionine
Summary for 6R8A
| Entry DOI | 10.2210/pdb6r8a/pdb |
| Related | 6R85 6R88 6R89 |
| Descriptor | Glutamate receptor 3.3,Glutamate receptor 3.3, METHIONINE, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | glutamate receptor-like, amino acid-binding, membrane protein |
| Biological source | Arabidopsis thaliana (thale cress) More |
| Total number of polymer chains | 4 |
| Total formula weight | 108499.00 |
| Authors | Alfieri, A.,Pederzoli, R.,Costa, A. (deposition date: 2019-04-01, release date: 2020-01-01, Last modification date: 2024-01-24) |
| Primary citation | Alfieri, A.,Doccula, F.G.,Pederzoli, R.,Grenzi, M.,Bonza, M.C.,Luoni, L.,Candeo, A.,Romano Armada, N.,Barbiroli, A.,Valentini, G.,Schneider, T.R.,Bassi, A.,Bolognesi, M.,Nardini, M.,Costa, A. The structural bases for agonist diversity in anArabidopsis thalianaglutamate receptor-like channel. Proc.Natl.Acad.Sci.USA, 117:752-760, 2020 Cited by PubMed Abstract: 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 increase in 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. PubMed: 31871183DOI: 10.1073/pnas.1905142117 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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