7lz2
From Proteopedia
(New page: '''Unreleased structure''' The entry 7lz2 is ON HOLD Authors: Description: Category: Unreleased Structures) |
|||
| (4 intermediate revisions not shown.) | |||
Current revision
Structure of glutamate receptor-like channel GLR3.4 ligand-binding domain in complex with methionine
Structural highlights
FunctionGLR34_ARATH Glutamate-gated receptor that probably acts as non-selective cation channel, at least in hypocotyls (Probable). Can be triggered by Asn, Ser, Gly and, to a lower extent, Ala, Cys and Glu (PubMed:18162597, PubMed:22447719). May be involved in light-signal transduction and calcium homeostasis via the regulation of calcium influx into cells (Probable). Plays an important role in the calcium-based fast transmission of environmental stress (PubMed:15864638). Acts as negative regulator of lateral root initiation and development (PubMed:23590882). May restrict primordia numbers and position along the root axis by a signaling process originating in the phloem (PubMed:23590882). AtGLR3.4-mediated cytosolic calcium influx may be involved in the regulation of seed germination under salt stress by modulating sodium accumulation through the SOS pathway (PubMed:29432559).[1] [2] [3] [4] [5] [6] [7] Publication Abstract from PubMedGlutamate receptor-like channels (GLRs) play vital roles in various physiological processes in plants, such as wound response, stomatal aperture control, seed germination, root development, innate immune response, pollen tube growth, and morphogenesis. Despite the importance of GLRs, knowledge about their molecular organization is limited. Here we use X-ray crystallography and single-particle cryo-EM to solve structures of the Arabidopsis thaliana GLR3.4. Our structures reveal the tetrameric assembly of GLR3.4 subunits into a three-layer domain architecture, reminiscent of animal ionotropic glutamate receptors (iGluRs). However, the non-swapped arrangement between layers of GLR3.4 domains, binding of glutathione through S-glutathionylation of cysteine C205 inside the amino-terminal domain clamshell, unique symmetry, inter-domain interfaces, and ligand specificity distinguish GLR3.4 from representatives of the iGluR family and suggest distinct features of the GLR gating mechanism. Our work elaborates on the principles of GLR architecture and symmetry and provides a molecular template for deciphering GLR-dependent signaling mechanisms in plants. Structure of the Arabidopsis thaliana glutamate receptor-like channel GLR3.4.,Green MN, Gangwar SP, Michard E, Simon AA, Portes MT, Barbosa-Caro J, Wudick MM, Lizzio MA, Klykov O, Yelshanskaya MV, Feijo JA, Sobolevsky AI Mol Cell. 2021 Jun 17. pii: S1097-2765(21)00409-3. doi:, 10.1016/j.molcel.2021.05.025. PMID:34161757[8] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
