PMID:12202833
| Citation |
Benoff, B, Yang, H, Lawson, CL, Parkinson, G, Liu, J, Blatter, E, Ebright, YW, Berman, HM and Ebright, RH (2002) Structural basis of transcription activation: the CAP-alpha CTD-DNA complex. Science 297:1562-6 |
|---|---|
| Abstract |
The Escherichia coli catabolite activator protein (CAP) activates transcription at P(lac), P(gal), and other promoters through interactions with the RNA polymerase alpha subunit carboxyl-terminal domain (alphaCTD). We determined the crystal structure of the CAP-alphaCTD-DNA complex at a resolution of 3.1 angstroms. CAP makes direct protein-protein interactions with alphaCTD, and alphaCTD makes direct protein-DNA interactions with the DNA segment adjacent to the DNA site for CAP. There are no large-scale conformational changes in CAP and alphaCTD, and the interface between CAP and alphaCTD is small. These findings are consistent with the proposal that activation involves a simple "recruitment" mechanism. |
| Links |
PubMed Online version:10.1126/science.1076376 |
| Keywords |
Crystallography, X-Ray; Cyclic AMP Receptor Protein/chemistry; Cyclic AMP Receptor Protein/metabolism; Cyclic AMP Receptor Protein/physiology; DNA/chemistry; DNA/metabolism; DNA-Directed RNA Polymerases/chemistry; DNA-Directed RNA Polymerases/metabolism; DNA-Directed RNA Polymerases/physiology; Macromolecular Substances; Models, Molecular; Nucleic Acid Conformation; Protein Binding; Protein Conformation; Structure-Activity Relationship; Transcription, Genetic; Transcriptional Activation |
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