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. 2020 Sep 30;117(41):25494–25504. doi: 10.1073/pnas.2010484117

Fig. 2.

Fig. 2.

Rev1 protein-templated DNA synthesis. (A) An active site close-up of the Rev1 intermediate crystal structure. The nucleic acid residues are shown in yellow and Rev1 in gray. An Fo–Fc OMIT map contoured at σ = 3.0 is shown as a green mesh. (B) A focused view of the structural movements in the Rev1 intermediate complex. The reactant and product states are indicated. The red arrows and distances (Å) highlight significant conformational differences. (C) An active site close-up of the Rev1 product complex after a 10-min soak in MgCl2. An Fo–Fc OMIT map contoured at σ = 3.0 is shown as a green mesh. (D) A focused view of the active site of the product complex (yellow sticks) with an overlay of the dCTP from the Rev1 ternary complex (gray sticks) shown for reference. Red arrows and distances (Å) are indicated to highlight significant movements. Plots of the steady-state kinetics for (E) R518A and (F) WT Rev1 are shown with the kcat and Km (dCTP) indicated for each graph. Steady-state kinetics were performed in triplicate.