Fig. 8
From: Time-lapse crystallography snapshots of a double-strand break repair polymerase in action
Comparison of the active sites of the pol μ and β product complexes. a Structurally equivalent residues: Arg323 (R323), Arg183 (R183); Gly320 (G320), Ser180 (S180); Asp332 (D332), Asp192 (D192); Asp330 (D330), Asp190 (D190); Asp418 (D418), Asp256 (D256); Arg416 (R416), Arg254 (R254). b Structurally distinct residues with possible overlapping roles: Lys438 (K438), Asp276 (D276); Lys325 (K325), Arg149 (R149); His329 (H329), Gly189 (G189); Trp434 (W434), Phe272 (F272). Pol μ is displayed in yellow stick, while pol β is in salmon stick representation. Structurally equivalent manganese atoms are shown in magenta and purple for pol β and pol μ, respectively. The DNA primer terminus is shown in cyan for pol μ and green for pol β
