Portal de Periódicos da CAPES

The structure of a CAP–DNA complex having two cAMP molecules bound to each monomer

1997; National Academy of Sciences; Volume: 94; Issue: 7 Linguagem: Inglês

10.1073/pnas.94.7.2843

1091-6490

J.M. Passner, Thomas A. Steitz,

Escherichia coli research studies

The 2.2 Å resolution crystal structure of the Escherichia coli catabolite gene activator protein (CAP) complexed with cAMP and a 46-bp DNA fragment reveals a second cAMP molecule bound to each protein monomer. The second cAMP is in the syn conformation and is located on the DNA binding domain interacting with the helix-turn-helix, a β-hairpin from the regulatory domain and the DNA (via water molecules). The presence of this second cAMP site resolves the apparent discrepancy between the NMR and x-ray data on the conformation of cAMP, and explains the cAMP concentration-dependent behaviors of the protein. In addition, this site’s close proximity to mutations affecting transcriptional activation and its water-mediated interactions with a DNA recognition residue (E181) and DNA raise the possibility that this site has biological relevance.