Fig. 2: Structure of the HSV-1 helicase subunit UL5 bound to ssDNA and ADP.
From: Structural and mechanistic insights into the herpes simplex virus type 1 helicase-primase primosome
a Cartoon representation of UL5 colored by domains as the schematic. The ssDNA is shown in cartoon and the ADP and Mg2+ are shown in spheres; electrostatic surface potential of UL5 (blue: electropositive; red: electronegative). ssDNA and ADP are shown as spheres. b The ATPase active site of UL5. ADP is cyan; Mg2+ is green. Polar contacts are indicated by yellow dashed lines. c Key residues binding the ssDNA. Polar contacts are indicated in blue dashed lines. d Helicase activity of the HSV-1 UL5–UL52–UL8 complex. UL5 mutations (Ser104Ala, Phe146Ala, Phe151 Ala, Arg505Ala, Arg507Ala) significantly reduced the complex’s helicase activity in vitro compared to wild type (WT). The data represent mean ± SD of three independent experiments.
