Fig. 2: Structure of XlVMAT2WT.
From: Engineering of a mammalian VMAT2 for cryo-EM analysis results in non-canonical protein folding
a Cryo-EM structure of XlVMAT2WT. Left, XlVMAT2WT (in spectrum color) viewed parallel to the membrane (gray rectangle). Right, XlVMAT2WT viewed perpendicular to the membrane from the cytosolic side. N- and C-domains are colored in blue and yellow, respectively. b Superposition of XlVMAT2WT C-domain (in yellow) onto XlVMAT2WT N-domain (in blue). c MST fitting curves of DA/SER/RSP binding to XlVMAT2WT, N = 3 repeats with biologically independent protein samples. Data are presented as mean ± SEM. Source data are provided as a Source Data file. d Solvent accessibility analysis and docking of SER in XlVMAT2WT (blue and yellow cartoons). The solvent-accessible space is displayed as red surface. Left, viewed parallel to the membrane. Right, viewed perpendicular to the membrane from the luminal side. Docked SER is displayed as cyan spheres. e Potential hydrophobic interactions between docked SER (cyan spheres) and XlVMAT2WT (blue and yellow cartoons). Participating residues are shown as sticks. f Potential polar interactions between docked SER (cyan sticks) and XlVMAT2WT (yellow cartoon) are indicated by black dashed lines. Participating residues are shown as yellow sticks. g MST fitting curves of SER binding to HsVMAT2 WT and variants as indicated, N = 3 repeats with biologically independent protein samples. Data are presented as mean ± SEM. Source data are provided as a Source Data file.
