Fig. 3

Fig. 3

Molecular details for H3_(1–9) readout by PHF14_PZP. (A) 2Fo−Fc omit map (blue meshes) around the H3 peptide (yellow sticks) is contoured at the 0.7σ level. PHD1 finger is shown as cyan ribbon. (B) Overall structure of the H3_(1–25)-PHF14_PZP complex. PHD1 finger (cyan), ZnK (light blue), PHD2 finger (light pink), and H3 peptide (yellow) are shown as ribbons. Zinc ions are depicted as white spheres. (C) Electrostatic surface view of PHF14_PZP bound to H3 peptides. Electrostatic potential is shown as a spectrum ranging from − 5 kT/e (red) to + 5 kT/e (blue). (D) Topology diagram of the H3_(1–9)-PHF14_PZP complex. Helices and strands are labelled and rainbow-colored from the N- (blue) to C- (red) termini. H3 is depicted in yellow and the insertion loop is highlighted in magenta. (E) Binding details of PHF14_PZP with H3 peptide. The PHD1 finger of PHF14_PZP is shown as a cyan and magenta (loop) ribbon. The residues of H3 peptide are depicted as yellow sticks. Key residues of PHF14_PZP are depicted as purple or cyan sticks. Green dashes and red dashes represent the hydrogen bonds and ionic bonds, respectively. (F) ITC fitting curves of PHF14_PZP mutants titrated with the H3_(1–15) peptide. N.D. = not detected. (G) ITC fitting curves of PHF14_PZP titrated with the H3_(1–15) peptide bearing different modifications. N.D. = not detected.