Figure 2
(a) Quaternary structure of the VSC tetramer with monomers A (grey), B (magenta), C (blue) and D (green). P, Q and R are the molecular axes of the tetramer as described by Fita et al. (1986), where the P axis is between monomers A–C and B–D, the R axis is between monomers A–B and C–D and the Q axis is perpendicular to P and R. Arrows indicate the major and minor channels. (b) Tertiary structure of the VSC monomer generated by Swiss-PdbViewer (Guex & Peitsch, 1997), with the N-terminal domain (residues 2–55) in red, the β-barrel domain (residues 56–301) in orange, the wrapping domain (residues 302–416) in yellow and the α-helical domain (417–484) in green. The observed protohaem IX (heme) and the modelled NADPH are coloured light grey. |