Fig. 2.

Crystal structure of Asf1N in complex with the C-terminus of Rad53(800-821). (A) Cartoon representation of Asf1 (in gray) bound to Rad53(800-821) in orange. Dashed lines are used to materialize the peptide chain between the two binding epitopes. Important Rad53 residues are labeled. (B) Detail of the interface delineated in (A). In the crystal structure, the peptide bridges epitopes on two different Asf1 molecules, but NMR solution analyses indicate that the peptide normally binds a single Asf1 molecule (see Supporting Information and Fig. S4). Hydrophobic side chains are shown as spheres, polar and charged residues as sticks. Polar contacts are shown as yellow dashed lines. Residue labels are indicated. (C) Cartoon representation of Asf1 (in gray) bound to the HirA B domain (in green) and to the H3 (in rose)-H4 (in magenta) complex. Residues overlapping with Rad53 are indicated.