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. 1997 Apr 1;94(7):2843–2847. doi: 10.1073/pnas.94.7.2843

Figure 4.

Figure 4

Comparison of part of the DNA binding domain (A) and the β-hairpin loop (B) structures of CAP complexed with only one cAMP per subunit (magenta) with that of CAP complexed with DNA and two cAMP molecules per subunit (cyan). (A) α-Carbon backbones of the small domains were superimposed. In the structure of CAP complexed with only one cAMP per subunit and without DNA, Arg-180 could hydrogen-bond with the phosphate of the syn-cAMP (yellow); whereas in the structure of CAP complexed with DNA and two cAMP molecules per subunit, Arg-180 hydrogen bonds to guanosine-7. (B) α-Carbon backbones of the large domains, excluding the β-hairpin loop, were superimposed, and the side chains for Lys-52, Asp-53, and Lys-57 are shown.