Extended Data Fig. 1: Domain organization of the HSV-1 HP complex and structures of individual subunits.
From: Structural and mechanistic insights into herpesvirus helicase–primase and its therapeutic inhibitors
a, Linear representations of amino acid sequences illustrating the domain organization of the three subunits in HSV-1 HP complex: UL8 (with exonuclease, palm, fingers, and thumb subdomains), UL5 helicase (with seven motifs), and UL52 domains (N-terminal, AEP domain, three motifs, and zinc finger motif), adapted from Bermek and Williams14. The sequences of the three motifs in UL52 are shown below, with the catalytic residues highlighted in red. b–d, Ribbon diagrams of individual subunits in the solved structure of the HSV-1 HP complex with AMNV, using the same color scheme as in a. The seven motifs in UL5 and the three motifs in UL52 are highlighted in red, with catalytic residues in UL52 represented as orange sticks. The putative C-terminal domain and ZnF motif of UL52, depicted in (a), are not resolved and therefore are not shown in (d). The UL5 1B domain is not labeled in (a).
