1lb2 | pdb_00001lb2

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

spinqualitylabelsall models 1lb2, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1lb2 is a 5 chain structure with sequence from Escherichia coli. The December 2003 RCSB PDB Molecule of the Month feature on Catabolite Activator Protein by David S. Goodsell is 10.2210/rcsb_pdb/mom_2003_12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.1Å Ligands: CMP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CRP_ECOLI This protein complexes with cyclic AMP and binds to specific DNA sites near the promoter to regulate the transcription of several catabolite-sensitive operons. The protein induces a severe bend in the DNA. Acts as a negative regulator of its own synthesis as well as for adenylate cyclase (cyaA), which generates cAMP. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Catabolite gene activator protein 3D structures RNA polymerase 3D structures

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