1lb2 | pdb_00001lb2
Structure of the E. coli alpha C-terminal domain of RNA polymerase in complex with CAP and DNA
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| 1lb2, resolution 3.1Å | |||||||||||||
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| Ligands: | CMP | ||||||||||||
| Activity: | DNA-directed RNA polymerase, with EC number 2.7.7.6 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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.
About this Structure
1LB2 is a Protein complex structure of sequences from Escherichia coli. The following page contains interesting information on the relation of 1LB2 with [Catabolite Activator Protein]. Full crystallographic information is available from OCA.
Reference
Structural basis of transcription activation: the CAP-alpha CTD-DNA complex., Benoff B, Yang H, Lawson CL, Parkinson G, Liu J, Blatter E, Ebright YW, Berman HM, Ebright RH, Science. 2002 Aug 30;297(5586):1562-6. PMID:12202833
Page seeded by OCA on Thu Mar 20 12:28:43 2008
