1G6N

2.1 ANGSTROM STRUCTURE OF CAP-CAMP

Replaces:  3GAPReplaces:  1GAP

Summary for 1G6N

• Entry DOI: 10.2210/pdb1g6n/pdb
• Related: 3GAP
• Descriptor: CATABOLITE GENE ACTIVATOR PROTEIN, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE (3 entities in total)
• Functional Keywords: catabolite activator protein (cap), camp receptor protein (crp), transcription, allostery, cyclic amp, camp, dna binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 48003.29

Authors

Passner, J.M.,Schultz, S.C.,Steitz, T.A. (deposition date: 2000-11-07, release date: 2000-12-15, Last modification date: 2023-08-09)

Primary citation

Passner, J.M.,Schultz, S.C.,Steitz, T.A.
Modeling the cAMP-induced allosteric transition using the crystal structure of CAP-cAMP at 2.1 A resolution.
J.Mol.Biol., 304:847-859, 2000

PubMed Abstract: After an allosteric transition produced by the binding of cyclic AMP (cAMP), the Escherichia coli catabolite gene activator protein (CAP) binds DNA specifically and activates transcription. The three-dimensional crystal structure of the CAP-cAMP complex has been refined at 2.1 A resolution, thus enabling a better evaluation of the structural basis for CAP phenotypes, the interactions of cAMP with CAP and the roles played by water structure. A review of mutational analysis of CAP together with the additional structural information presented here suggests a possible mechanism for the cAMP-induced allostery required for DNA binding and transcriptional activation. We hypothesize that cAMP binding may reorient the coiled-coil C-helices, which provide most of the dimer interface, thereby altering the relative positions of the DNA-binding domains of the CAP dimer. Additionally, cAMP binding may cause a further rearrangement of the DNA-binding and cAMP-binding domains of CAP via a flap consisting of beta-strands 4 and 5 which lies over the cAMP.

PubMed: 11124031
DOI: 10.1006/jmbi.2000.4231

Experimental method

X-RAY DIFFRACTION (2.1 Å)