Structure of the Arabidopsis thaliana glutamate receptor-like channel GLR3.4
Published on 06.22.2021 in Molecular Cell
Marriah N. Green, Shanti Pal Gangwar, Erwan Michard, Alexander A. Simon, Maria Teresa Portes, Juan Barbosa-Caro, Michael M. Wudick, Michael A. Lizzio, Oleg Klykov, Maria V. Yelshanskaya, José A. Feijó, Alexander I. Sobolevsky
Cryo-EM structure of Arabidopsis thaliana glutamate receptor-like channel GLR3.4
Glutathione regulates channel activity by binding to C205 in amino-terminal domain
Crystal structures of GLR3.4 ligand-binding domain illustrate ligand promiscuity
Amino-terminal and ligand-binding domain layers show non-swapped domain arrangement
Glutamate 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.