Figure 4.
FIGURE 4. Overlay of the NH[2]-terminal domains of both
CprK structures. An overlay is shown that was created by
superimposition of the B and C -helices of both
ligand-free CprK and the CHPA-bound CprK structures with central
helices colored blue for both structures, while the
NH[2]-terminal -barrel (residues 20-108
for both structures) is colored green for the CHPA-CprK complex
and orange for the ligand free CprK. Bound CHPA molecules in the
CHPA-CprK structure are represented in atom-colored spheres. To
illustrate the motion of the NH[2]-terminal -barrel with respect to
the putative position of the HTH motifs in the DNA binding state
(by analogy to CRP), the putative HTH motifs are represented in
gray.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2006,
281,
28318-28325)
copyright 2006.
-helices of both
ligand-free CprK and the CHPA-bound CprK structures with central
helices colored blue for both structures, while the
NH[2]-terminal 
-barrel (residues 20-108
for both structures) is colored green for the CHPA-CprK complex
and orange for the ligand free CprK. Bound CHPA molecules in the
CHPA-CprK structure are represented in atom-colored spheres. To
illustrate the motion of the NH[2]-terminal