Figure 1 - full size

 

Figure 1.
(a) Ribbon diagram of the JMJD2A–NOG–H3K36me3 complex, with the JmjN domain (yellow), -hairpin and mixed region (red), JmjC domain (blue) and C-terminal domain (green) depicted. NOG and H3K36me3 peptide are rendered as sticks with green and cyan carbon atoms, respectively; Ni(II) and Zn(II) atoms are in orange and gray, respectively. (b) Electrostatic surface of JMJD2A bound to KG (green carbons) and the H3K9me3 peptide (yellow carbons). Electrostatic potential is contoured from +10 k[b]T e^-1 (blue) to -10 k[b]T e^-1 (red). (c,d) Stereo views of simulated annealing F[o] - F[c] omit maps of the bound H3K36me3 (c) and H3K9me3 (d) peptides. Electron density is contoured at 2.0 . JMJD2A carbon atoms are in gray; hydrogen bonds are shown as orange dashed lines. (e,f) Schematics of the interactions between JMJD2A and the H3K36me3 (e) and H3K9me3 (f) substrates. Residues engaging in van der Waals interactions (open ellipses) and hydrogen-bonding (filled ellipses) with the histone H3 peptides are colored as in a.

The above figure is reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2007, 14, 689-695) copyright 2007.