PMID:15102444
| Citation |
Lawson, CL, Swigon, D, Murakami, KS, Darst, SA, Berman, HM and Ebright, RH (2004) Catabolite activator protein: DNA binding and transcription activation. Curr. Opin. Struct. Biol. 14:10-20 |
|---|---|
| Abstract |
Recently determined structures of the Escherichia coli catabolite activator protein (CAP) in complex with DNA, and in complex with the RNA polymerase alpha subunit C-terminal domain (alphaCTD) and DNA, have yielded insights into how CAP binds DNA and activates transcription. Comparison of multiple structures of CAP-DNA complexes has revealed the contributions of direct and indirect readout to DNA binding by CAP. The structure of the CAP-alphaCTD-DNA complex has provided the first structural description of interactions between a transcription activator and its functional target within the general transcription machinery. Using the structure of the CAP-alphaCTD-DNA complex, the structure of an RNA polymerase-DNA complex, and restraints from biophysical, biochemical and genetic experiments, it has been possible to construct detailed three-dimensional models of intact class I and class II transcription activation complexes. |
| Links |
PubMed PMC2765107 Online version:10.1016/j.sbi.2004.01.012 |
| Keywords |
Cyclic AMP Receptor Protein/metabolism; DNA/genetics; DNA/metabolism; DNA-Directed RNA Polymerases/metabolism; Escherichia coli; Models, Genetic; Models, Molecular; Promoter Regions, Genetic/genetics; Structure-Activity Relationship; Transcriptional Activation/genetics |
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