Extended Data Fig. 6: HSV-1 UL5 shares a conserved catalytic fold with other SF1 family helicases.
From: Structural and mechanistic insights into herpesvirus helicase–primase and its therapeutic inhibitors
a, Structural comparison of UL5 with other SF1 helicases bound to ATP analogues and DNA substrates. Shown are UL5 (upper left), ScPif1 with ADP·AlF4-ssDNA (upper right)55, RecD2 with ADPNP and ssDNA (lower left)27, and uvrD with ADP·AlF3 and DNA (lower right)56. All structures are displayed as grey ribbon diagrams, with UL5’s seven motifs highlighted in red. The corresponding seven motifs in other helicases are shown in distinct colors, and approximately aligned with UL5’s seven motifs. ATP analogues are depicted as colored sticks, Mg2+ ions as spheres, and DNA backbones and individual bases as sticks in unique colors for clarity. b, Comparison of the active sites of UL5 and other helicases depicted in (a). The superimposition is based on the seven conserved motifs of UL5 and equivalent motifs in other SF1 helicases, with consistent color scheme and style as in (a).
