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Structure paper

TitleStructure of the Arabidopsis thaliana glutamate receptor-like channel GLR3.4.
Journal, issue, pagesMol Cell, Vol. 81, Issue 15, Page 3216-33226.e8, Year 2021
Publish dateAug 5, 2021
AuthorsMarriah 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 /
PubMed AbstractGlutamate 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 ...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.
External linksMol Cell / PubMed:34161757 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.5 - 4.39 Å
Structure data

23606

7lzh

EMDB-23606, PDB-7lzh:
Structure of the glutamate receptor-like channel AtGLR3.4
Method: EM (single particle) / Resolution: 3.57 Å

23607

7lzi

EMDB-23607, PDB-7lzi:
Structure of the glutamate receptor-like channel AtGLR3.4
Method: EM (single particle) / Resolution: 4.39 Å

PDB-7lz0:
Structure of glutamate receptor-like channel GLR3.4 ligand-binding domain in complex with glutamate
Method: X-RAY DIFFRACTION / Resolution: 2.29 Å

PDB-7lz1:
Structure of glutamate receptor-like channel GLR3.4 ligand-binding domain in complex with serine
Method: X-RAY DIFFRACTION / Resolution: 1.51 Å

PDB-7lz2:
Structure of glutamate receptor-like channel GLR3.4 ligand-binding domain in complex with methionine
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-GLU:
GLUTAMIC ACID / Glutamic acid

ChemComp-CL:
Unknown entry / Chloride

ChemComp-SO4:
SULFATE ION / Sulfate

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-HOH:
WATER / Water

ChemComp-SER:
SERINE / Serine

ChemComp-MET:
METHIONINE / Methionine

ChemComp-NA:
Unknown entry

ChemComp-BME:
BETA-MERCAPTOETHANOL / 2-Mercaptoethanol

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-GSH:
GLUTATHIONE / Glutathione

Source
  • arabidopsis thaliana (thale cress)
KeywordsMEMBRANE PROTEIN / Arabidopsis thaliana / Ion-Channel / glutamate receptor-like channel (GLR) / Ligand binding domain / TRANSPORT PROTEIN

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