Fig. 2
Nsp1 has a larger interaction interface with Polα than the wHTH domain of RPA. (A) and (B), analysis of potential hydrogen bonds at the wHTH-Polα and Nsp1-Polα interfaces, respectively. Nsp1, wHTH, and Polα are represented as cartoons and colored green, cyan, and salmon, respectively. H-bonds are depicted as dark-blue dashed lines. A position of the Lys599 side-chain was adjusted for optimal H-bond formation with Gly49 (C) and (D), analysis of potential hydrophobic contacts at the wHTH-Polα and Nsp1-Polα interfaces, respectively. Polα is represented as a surface. Polα residues, involved in hydrophobic interactions with Nsp1 or wHTH, are shown as sticks and colored salmon. Nsp1 and wHTH are represented as ribbon and colored green and cyan, respectively. Their residues, involved in hydrophobic interactions with Polα, are shown as sticks. PyMol Molecular Graphics System and the coordinates of Nsp1/primosome and RPAcore/PolαCD/DNA complexes were used for figure preparation (pdb codes 7opl and 9mj5, respectively).
