Fig. 1: Cryo-EM structure of the PV3-SC8GPP3+GSH complex.
a Three-dimensional reconstruction of PV3-SC8 VLP after incubation with a molar excess of GSH and GPP3. The VLP is viewed along the icosahedral twofold symmetry axis with the VP1, VP0 and VP3 subunits of the capsid protomer coloured light blue, light green and light red, respectively. A single capsid protomer is coloured in a darker shade, GSH magenta and GPP3 orange. b Close-up view looking down the icosahedral fivefold symmetry axis, coloured as in a showing GSH bound at an interprotomer interface. c Close-up view along the fivefold axis of the apo PV3-SC8 VLP reconstruction (EMD-15543) showing the absence of features for GSH. d Cartoon representation of two neighbouring capsid protomers; protomer A is coloured as in a, protomer B is coloured grey, GSH magenta and GPP3 orange. The cryo-EM map is depicted as a semi-transparent surface. e Cryo-EM electron potential map with GSH fitted as a stick model and elemental colouring for oxygen (red), nitrogen (blue) and sulfur (yellow). The map is displayed at a contour level of 1.2 σ (σ is the standard deviation of the electron potential map). f Cartoon depiction of the VP1 hydrophobic pocket with bound GPP3 fitted into the cryo-EM potential map. The electron potential map for GPP3 is shown at 1.5 σ. All electron potential map images are rendered at a radius of 2 Å around atoms.
