Figure 3

The Dbf4 peptide binds to the hydrophobic surface opposite to the pS/T-binding pocket. (a) Structure of the PBD of Cdc5 in the presence of the Dbf4 peptide. The Fo-Fc>0 electron density map around the hydrophobic pocket opposite to the phosphopeptide binding site is shown as a yellow mesh contoured at 2.5σ with a tetrapeptide modelled for reference (yellow sticks). (b) Isothermal calorimetry data and analysis for the titration of the Dbf4 into the polo-box domain of Cdc5PBD (left) or Cdc5 PBD-A567W (right).