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Figure 1.
Figure 1. Structures of the Free yHst2/ADP-HPD/Histone H4
Complex
(A) Ternary yHst2 (gray) complex, highlighting
strictly conserved (red) and conserved (pink) residues; the
binding sites of acetyl-lysine (green), carba-NAD^+ (cyan), and
ADP-ribose (yellow); and the conserved C and D pockets.
Hydrogen bonds between the acetyl-lysine and carba-NAD^+ are
shown as yellow dotted lines. Residues 43–48 of the flexible
loop and residue 64 were omitted for clarity.
(B)
Superimposition of the yHst2/ADP-ribose/H4 complex (magenta)
with the yHst2/ADP-HPD/H4 complex (cyan) and the
yHst2/ADP-HPD/H4 complex bound to nicotinamide (blue). The
intermediate analog, acetylated histone H4 ligands, and
nicotinamide are shown in green for the ADP-ribose complex,
yellow for the free ADP-HPD complex, and orange for the
nicotinamide-bound ADP-HDP complex.
(C) Simulated annealing
omit density contoured at 1.0 σ showing density for the protein
(blue) and ADP-HPD (atoms individually colored). Water molecules
are shown as blue spheres.
(D) yHst2 bound to ADP-HPD
(atoms individually colored) and highlighting residues that make
hydrogen bonds (red dashed lines) or van der Waals contacts with
ADP-HPD. Hydrogen bonding residues are colored pink, residues
that make van der Waals interactions are colored cyan, and
residues that make both interactions are colored purple.
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