6VEA

Structure of the Glutamate-Like Receptor GLR3.2 ligand-binding domain in complex with Glycine

6VEA の概要

• エントリーDOI: 10.2210/pdb6vea/pdb
• 分子名称: Glutamate receptor 3.2, GLYCINE, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: ligand-binding domain, glutamate like receptor, ion channel, arabidopsis, membrane protein
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34032.42

構造登録者

Gangwar, S.P.,Green, M.N.,Yoder, J.B.,Sobolevsky, A.I. (登録日: 2019-12-30, 公開日: 2020-09-23, 最終更新日: 2023-10-11)

主引用文献

Gangwar, S.P.,Green, M.N.,Michard, E.,Simon, A.A.,Feijo, J.A.,Sobolevsky, A.I.
Structure of the Arabidopsis Glutamate Receptor-like Channel GLR3.2 Ligand-Binding Domain.
Structure, 29:161-, 2021

PubMed Abstract: Glutamate receptor-like channels (GLRs) play important roles in numerous plant physiological processes. GLRs are homologous to ionotropic glutamate receptors (iGluRs) that mediate neurotransmission in vertebrates. Here we determine crystal structures of Arabidopsis thaliana GLR3.2 ligand-binding domain (LBD) in complex with glycine and methionine to 1.58- and 1.75-Å resolution, respectively. Our structures show a fold similar to that of iGluRs, but 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 mutation R133A strongly increases the constitutive activity of the channel, suggesting that the LBD mutated at the residue critical for agonist binding produces a more stable closed clamshell conformation. Furthermore, our structures explain the promiscuity of GLR activation by different amino acids, confirm evolutionary conservation of structure between GLRs and iGluRs, and predict common molecular principles of their gating mechanisms driven by bilobed clamshell-like LBDs.

PubMed: 33027636
DOI: 10.1016/j.str.2020.09.006

実験手法

X-RAY DIFFRACTION (1.58 Å)