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• W2085198247 endingPage "2847" @default.
• W2085198247 startingPage "2843" @default.
• W2085198247 abstract "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." @default.
• W2085198247 created "2016-06-24" @default.
• W2085198247 creator A5005980770 @default.
• W2085198247 creator A5050923234 @default.
• W2085198247 date "1997-04-01" @default.
• W2085198247 modified "2023-10-11" @default.
• W2085198247 title "The structure of a CAP–DNA complex having two cAMP molecules bound to each monomer" @default.
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• W2085198247 doi "https://doi.org/10.1073/pnas.94.7.2843" @default.
• W2085198247 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/20284" @default.
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