Figure 7.
FIGURE 7. Binding of ortho-chlorophenolic compounds causes
structural rearrangement. A, overlay of a single CHPA-binding
site of the ligand-free CprK (color coding same as described for
Fig. 1) with a hybrid CprK structure (in gray; see "Results and
Discussion"). This clearly illustrates the induced fit in both
the NH[2]-terminal -barrel and the C helix
residues upon binding of CHPA. B, similar view to A, but only
the hybrid structure is displayed, colored-coded as described
for Fig. 1. The hydrophobic pocket created by the C helix
residues is depicted as a transparent surface. H-bonds between
CHPA and CprK are depicted in dashed lines. No direct
interaction can be made between CHPA and Lys-133, while the CHPA
chloride atom is not ideally placed in the binding pocket. C,
similar view to B but for the CHPA-CprK crystal structure. The
reorientation of the -barrel has allowed for
an additional interaction between CHPA and Lys-133 while
positioning the CHPA chloride atom in the center of the
hydrophobic cavity.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2006,
281,
28318-28325)
copyright 2006.
-barrel and the C helix
residues upon binding of CHPA. B, similar view to A, but only
the hybrid structure is displayed, colored-coded as described
for Fig. 1. The hydrophobic pocket created by the C helix
residues is depicted as a transparent surface. H-bonds between
CHPA and CprK are depicted in dashed lines. No direct
interaction can be made between CHPA and Lys-133, while the CHPA
chloride atom is not ideally placed in the binding pocket. C,
similar view to B but for the CHPA-CprK crystal structure. The
reorientation of the