Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 304, Issue 5, Pages 847-859Publisher
ACADEMIC PRESS LTD
DOI: 10.1006/jmbi.2000.4231
Keywords
catabolite activator protein (CAP); cAMP receptor protein (CRP); transcription; allostery; X-ray crystallography
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Funding
- NIGMS NIH HHS [GM22778] Funding Source: Medline
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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 Angstrom 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. (C) 2000 Academic Press.
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