2cgp: Difference between revisions

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[[Image:2cgp.gif|left|200px]]
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{{STRUCTURE_2cgp|  PDB=2cgp  |  SCENE=  }}  
{{STRUCTURE_2cgp|  PDB=2cgp  |  SCENE=  }}  


'''CATABOLITE GENE ACTIVATOR PROTEIN/DNA COMPLEX, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE'''
===CATABOLITE GENE ACTIVATOR PROTEIN/DNA COMPLEX, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_9096308}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_9096308}}


==About this Structure==
==About this Structure==
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[[Category: Camp-binding]]
[[Category: Camp-binding]]
[[Category: Dna-binding]]
[[Category: Dna-binding]]
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