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.
-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