RT Journal Article
SR Electronic
T1 Structure of the Glutamate-Like Receptor GLR3.2 ligand-binding domain
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2019.12.23.887497
DO 10.1101/2019.12.23.887497
A1 Shanti Pal Gangwar
A1 Marriah Green
A1 Alexander I. Sobolevsky
YR 2019
UL http://biorxiv.org/content/early/2019/12/24/2019.12.23.887497.abstract
AB Glutamate-like receptors (GLRs) in plants play an important role in a number of physiological processes, including wound response, stomatal aperture control, seed germination, root development, innate immune responses, pollen tube growth and morphogenesis. GLRs share amino acid sequence similarity with ionotropic glutamate receptors (iGluRs) that mediate neurotransmission in the nervous system of vertebrates. In contrast to iGluRs, however, for which numerous full-length structures are available, the structural information about the plant GLRs has been missing. Here we determine crystal structures of Arabidopsis thaliana GLR3.2 ligand-binding domain (LBD) in complex with glycine and methionine to 1.57 and 1.86 Å resolution, respectively. Our structures show a fold similar to iGluRs, with several secondary structure elements either missing or different. The closed clamshell conformation of GLR3.2 LBD suggests that both glycine and methionine act as agonists. The structures reveal molecular determinants of ligand binding and explain the promiscuity of GLRs’ ligand activation compared to iGluRs. Structural similarities of LBDs confirm an evolutionary relationship between GLRs and iGluRs and predict common molecular principles of their gating mechanisms that are driven by the bilobed clamshell-like LBDs.