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Structure paper

TitleStructural insights into the activation of metabotropic glutamate receptors.
Journal, issue, pagesNature, Vol. 566, Issue 7742, Page 79-84, Year 2019
Publish dateJan 23, 2019
AuthorsAntoine Koehl / Hongli Hu / Dan Feng / Bingfa Sun / Yan Zhang / Michael J Robertson / Matthew Chu / Tong Sun Kobilka / Toon Laeremans / Jan Steyaert / Jeffrey Tarrasch / Somnath Dutta / Rasmus Fonseca / William I Weis / Jesper M Mathiesen / Georgios Skiniotis / Brian K Kobilka /
PubMed AbstractMetabotropic glutamate receptors are family C G-protein-coupled receptors. They form obligate dimers and possess extracellular ligand-binding Venus flytrap domains, which are linked by cysteine-rich ...Metabotropic glutamate receptors are family C G-protein-coupled receptors. They form obligate dimers and possess extracellular ligand-binding Venus flytrap domains, which are linked by cysteine-rich domains to their 7-transmembrane domains. Spectroscopic studies show that signalling is a dynamic process, in which large-scale conformational changes underlie the transmission of signals from the extracellular Venus flytraps to the G protein-coupling domains-the 7-transmembrane domains-in the membrane. Here, using a combination of X-ray crystallography, cryo-electron microscopy and signalling studies, we present a structural framework for the activation mechanism of metabotropic glutamate receptor subtype 5. Our results show that agonist binding at the Venus flytraps leads to a compaction of the intersubunit dimer interface, thereby bringing the cysteine-rich domains into close proximity. Interactions between the cysteine-rich domains and the second extracellular loops of the receptor enable the rigid-body repositioning of the 7-transmembrane domains, which come into contact with each other to initiate signalling.
External linksNature / PubMed:30675062 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3.262 - 7.9 Å
Structure data

0345

6n51

EMDB-0345, PDB-6n51:
Metabotropic Glutamate Receptor 5 bound to L-quisqualate and Nb43
Method: EM (single particle) / Resolution: 4.0 Å

0346

6n52

EMDB-0346, PDB-6n52:
Metabotropic Glutamate Receptor 5 Apo Form
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-0347:
Apo form metabotropic glutamate receptor 5 with Nanobody 43
Method: EM (single particle) / Resolution: 7.9 Å

PDB-6n4x:
Metabotropic Glutamate Receptor 5 Apo Form Ligand Binding Domain
Method: X-RAY DIFFRACTION / Resolution: 4.0 Å

PDB-6n4y:
Metabotropic Glutamate Receptor 5 Extracellular Domain with Nb43
Method: X-RAY DIFFRACTION / Resolution: 3.262 Å

PDB-6n50:
Metabotropic Glutamate Receptor 5 Extracellular Domain in Complex with Nb43 and L-quisqualic acid
Method: X-RAY DIFFRACTION / Resolution: 3.751 Å

Chemicals

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

ChemComp-MG:
Unknown entry

ChemComp-QUS:
(S)-2-AMINO-3-(3,5-DIOXO-[1,2,4]OXADIAZOLIDIN-2-YL)-PROPIONIC ACID / agonist*YM / Quisqualic acid

Source
  • homo sapiens (human)
  • lama glama (llama)
KeywordsMEMBRANE PROTEIN / Cell Surface Receptor / Cell Surface Receptor Nanobody / SIGNALING PROTEIN

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