Fig. 3: Rev1/DNA/dGTP 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/dGTP ternary complex. Key protein and DNA residues are shown as yellow sticks. The nucleotide binding (Can) metal and water molecule that replaces the catalytic metal (Cac) are shown as a green and blue sphere, respectively. A Polder OMIT map contoured at σ = 3.0 for the incoming dGTP is shown as a green mesh. b Two focused views of the hydrogen bonds formed between Rev1 R324 and the incoming dGTP. Hydrogen bonds are shown as black dashed lines and hydrogen bonding distances (Å) are labeled. c An overlay of the Rev1/DNA/dGTP ternary complex (yellow sticks) and Rev1/DNA/dCTP ternary complex (gray sticks) showing differences in the dNTP bases. Red arrows and distances (Å) highlight key differences between the two structures. The nucleotide binding (Can) and catalytic (Cac) metals are shown as spheres. d An overlay of the Rev1/DNA/dGTP ternary complex (yellow 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.
