Dynamic Fluctuations Provide the Basis of a Conformational Switch Mechanism in Apo Cyclic AMP Receptor Protein
Figure 5
The alignment of MD cluster best members of apo CRP monomer/dimer and holo CRP.
The superimposed MD best member structures of the clusters generated from three apo CRP monomer runs (A, B, C), three apo CRP dimer runs (D, E, F) and a holo CRP run (G) with a cluster radius of 3.5 Å. Colors of the structures match the colors of the clusters given in RMSD plots of cluster evolution in time (Figure S3). For example, the structure in cyan is the cluster best member no. 3, which is also colored in cyan. The white structures are the starting conformations for each run.