Summary information and primary citation

PDB-id
1lb2; SNAP-derived features in text and JSON formats; DNAproDB
Class
gene regulation-DNA
Method
X-ray (3.1 Å)
Summary
Structure of the e. coli alpha c-terminal domain of RNA polymerase in complex with cap and DNA
Reference
Benoff B, Yang H, Lawson CL, Parkinson G, Liu J, Blatter E, Ebright YW, Berman HM, Ebright RH (2002): "Structural basis of transcription activation: the CAP-alpha CTD-DNA complex." Science, 297, 1562-1566. doi: 10.1126/science.1076376.
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.

Cartoon-block schematics in six views (download the tarball)

PyMOL session file Download PDB file View in 3Dmol.js