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. 2023 Oct 4;24(19):14896. doi: 10.3390/ijms241914896

Figure 3.

Figure 3

RecA protein within the recombination filament. (A) Dynamic behavior of a RecA protein embedded in a RecA-ATP filament during a 200 ns molecular dynamic simulation, represented by the superposition of snapshots taken every 25 ns; regions that show higher flexibility (see typical RMSF plot in insert limited to the 1–333 region, adapted from [50]) are color-coded according to the labels and the dotted lines in the insert. (B) RecA-RecA interface change upon ATP hydrolysis. top panel: two filament forms observed in the presence of non-hydrolyzable ATP analogs (red, left), ADP or no cofactor (blue, right); monomers are colored alternatively with light and dark shades; bottom panel: two interacting monomers are represented in each view, with the bottom monomer in cartoon (N-terminal domain in purple, C-terminal domain in pink, ATPase domain in white) and the upper monomer in surface representation. The binding geometry in the left panel corresponds to the ATP-bound geometry (ATP is embedded in the interface) while the right panel shows the binding geometry corresponding to ADP as a cofactor or no cofactor.