Fig. 2: Rev1/DNA/dTTP 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/dTTP ternary complex. Key protein and DNA residues are shown as blue 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 dTTP is shown as a green mesh. b Two focused views of the hydrogen bonds formed between Rev1 R324 and the incoming dTTP. Hydrogen bonds are shown as black dashed lines and hydrogen bonding distances are labeled. c An overlay of the Rev1/DNA/dTTP ternary complex (light blue sticks) and Rev1/DNA/dCTP ternary complex (gray sticks). Red arrows and the respective distances (Å) highlight key active site differences between the two structures. The nucleotide binding (Can) and catalytic (Cac) metals are shown as spheres.
