Role of Flexibility in Protein-DNA-Drug Recognition: The Case of Asp677Gly-Val703Ile Topoisomerase Mutant Hypersensitive to Camptothecin
Figure 5
Overlap of 50 snapshots extracted every 200 ps for the wild-type (a) and the double mutant enzyme (b) trajectories. The structures have been superimposed on the Cα atoms of the active site residues Arg488, Arg590, and Tyr723. The “nose cone helices” are indicated by an arrow. The sites of the two mutations on the linker domain are highlighted by a red sphere in the mutant structure.
