2CGP

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

Summary for 2CGP

• Entry DOI: 10.2210/pdb2cgp/pdb
• Descriptor: DNA (5'-D(*GP*TP*CP*AP*CP*AP*TP*TP*AP*AP*T)-3'), DNA (5'-D(*AP*TP*TP*AP*AP*TP*GP*TP*GP*AP*CP*AP*TP*AP*T)-3'), PROTEIN (CATABOLITE GENE ACTIVATOR PROTEIN), ... (5 entities in total)
• Functional Keywords: complex (transcription regulation-dna), dna-binding, camp-binding, activator, transcription-dna complex, transcription/dna
• Biological source: Escherichia coli
• Total number of polymer chains: 3
• Total formula weight: 32270.09

Authors

Passner, J.M.,Steitz, T.A. (deposition date: 1997-01-31, release date: 1998-02-04, Last modification date: 2023-08-02)

Primary citation

Passner, J.M.,Steitz, T.A.
The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer.
Proc.Natl.Acad.Sci.USA, 94:2843-2847, 1997

PubMed Abstract: 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.

PubMed: 9096308
DOI: 10.1073/pnas.94.7.2843

Experimental method

X-RAY DIFFRACTION (2.2 Å)