1LB2

Structure of the E. coli alpha C-terminal domain of RNA polymerase in complex with CAP and DNA

Summary for 1LB2

• Entry DOI: 10.2210/pdb1lb2/pdb
• Descriptor: 5'-D(*CP*TP*TP*TP*TP*TP*TP*CP*CP*TP*AP*AP*AP*AP*TP*GP*TP*GP*AP*T)-3', 5'-D(*CP*TP*AP*GP*AP*TP*CP*AP*CP*AP*TP*TP*TP*TP*AP*GP*GP*AP*AP*AP*AP*AP*AP*G)-3', CATABOLITE GENE ACTIVATOR PROTEIN, ... (6 entities in total)
• Functional Keywords: protein-dna complex, gene-regulatory, gene regulation-dna complex, gene regulation/dna
• Biological source: Escherichia coli; More
• Total number of polymer chains: 5
• Total formula weight: 56098.84

Authors

Benoff, B.,Yang, H.,Lawson, C.L.,Parkinson, G.,Liu, J.,Blatter, E.,Ebright, Y.W.,Berman, H.M.,Ebright, R.H. (deposition date: 2002-04-01, release date: 2002-09-06, Last modification date: 2023-08-16)

Primary citation

Benoff, B.,Yang, H.,Lawson, C.L.,Parkinson, G.,Liu, J.,Blatter, E.,Ebright, Y.W.,Berman, H.M.,Ebright, R.H.
Structural basis of transcription activation: the CAP-alpha CTD-DNA complex.
Science, 297:1562-1566, 2002

PubMed 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.

PubMed: 12202833
DOI: 10.1126/science.1076376

Experimental method

X-RAY DIFFRACTION (3.1 Å)