2cgp
From Proteopedia
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CATABOLITE GENE ACTIVATOR PROTEIN/DNA COMPLEX, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE
Overview
The 2.2 A 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 beta-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.
About this Structure
2CGP is a Single protein structure of sequence from Escherichia coli with CMP as ligand. Full crystallographic information is available from OCA.
Reference
The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer., Passner JM, Steitz TA, Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):2843-7. PMID:9096308
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