Stepwise activation of a metabotropic glutamate receptor

Metabotropic glutamate receptors belong to a family of G protein-coupled receptors that are obligate dimers and possess a large extracellular ligand-binding domain that is linked via a cysteine-rich domain to their 7-transmembrane domain. Upon activation, these receptors undergo a large conformational change to transmit the ligand binding signal from the extracellular ligand-binding domain to the G protein-coupling 7-transmembrane domain.

Kaavya Krishna Kumar, Haoqing Wang, Chris Habrian, Jun Xu, Evan S. O’Brien, Elizabeth Montabana, Antoine Koehl & Brian K. KobilkaNaomi R. Latorraca, Susan Marqusee & Ehud Y. IsacoffK.K.K. and B.K.K. conceived the project. K.K.K. prepared samples, froze grids and collected cryo-EM data with help from C.Z. and E.M. K.K.K. and J.X. developed the minimal cysteine mGlu5 construct and performed bimane studies, and made smFRET samples with help from E.S.O. H.W.

Workflow of cryo-EM data processing to obtain CDPPB, Quis-bound mGlu5 structure, Intermediate 3a. Also shown is the density for Quis and CDPPB, with density also shown for residues around the ligands. Local resolution maps of the CDPPB, Quis-bound mGlu5 structure. Angular particle distribution of the structure. Gold-standard FSC curves of the Quis-bound mGlu5 structure. Workflow of cryo-EM data processing to obtain CDPPB-bound mGlu5 Intermediate 1b structure.

– FRET histogram with three component Gaussian fits for each ligand condition. Percentage area under the peak and peak center values. Apo , Quis , Quis + CDPPB , Quis + G Plot of the Akaike information criterion values for analysis with 1 to 5 Gaussians fits for the smFRET data. The AICc values showed broad minima at 3 and 4 fits. Three Gaussians were used to fit the data. smFRET data showing the comparison of Apo and antagonist-bound mGlu5 . Data represented as mean ± s.e.m.

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