Fig. 4: Rev1/DNA/dATP ternary complex structure.
From: Mechanism of nucleotide discrimination by the translesion synthesis polymerase Rev1
a An overall structure (left) and active site closeup (right) of the Rev1/DNA/dATP ternary complex. Key protein and DNA residues are shown as pink sticks. The nucleotide binding (Can) and catalytic (Cac) metals are shown as green spheres. A Polder OMIT map contoured at σ = 3.0 for the incoming dATP is shown as a green mesh. b Two focused views of the hydrogen bonds formed between Rev1 R324 and the incoming dATP (conformation 1). Hydrogen bonds are shown as black dashed lines and hydrogen bonding distances (Å) are labeled. c Two focused views of the hydrogen bonds formed between Rev1 R324 and the incoming dATP (conformation 2). Hydrogen bonds are shown as black dashed lines and hydrogen bonding distances (Å) are labeled. d An overlay of the Rev1/DNA/dATP ternary complex (conformation 1, pink sticks) and Rev1/DNA/dCTP ternary complex (gray sticks) showing differences in the position of the primer terminal dG 3′-OH. Red arrows and the respective distances (Å) show the movement of the primer terminal dG 3′-OH between the two structures. e An overlay of the Rev1/DNA/dATP ternary complex (conformation 2, pink sticks) and Rev1/DNA/dCTP ternary complex (gray sticks) showing differences in the position of the primer terminal dG 3′-OH. Red arrows and the respective distances (Å) show the movement of the primer terminal dG 3′-OH between the two structures.
