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Figure 3.
The interaction between HpFabZ and inhibitors. (A,B) Binding
positions of quercetin (salmon), apigenin (yellow), and
(S)-sakuranetin (purple-blue) around the tunnel entrance (model
A) or near the catalytic residues (model B) are shown. In model
A, the inhibitors bind to the entrance of tunnel B linearly
through hydrophobic interactions and are stacked between
residues Tyr100 and Pro112[prime prime or minute]. In model B,
inhibitors embed into tunnel C near the catalytic residues and
are located in the hydrophobic pocket. The electrostatic surface
of the active tunnel is rendered by a color ramp from red to
blue. (C --H) Quercetin colored in wheat (C,D), apigenin colored
in yellow (E,F), and (S)-sakuranetin colored in olive (G,H)
interact with surrounding residues and water molecules in
HpFabZ. Hydrogen bonds are shown as black dashes. Residues are
labeled and colored in green, cyan, magenta, and orange for
monomers A, B, C, and D, respectively.
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