1XS9
A MODEL OF THE TERNARY COMPLEX FORMED BETWEEN MARA, THE ALPHA-CTD OF RNA POLYMERASE AND DNA
Replaces: 1TI9Summary for 1XS9
Entry DOI | 10.2210/pdb1xs9/pdb |
Descriptor | 5'-D(P*GP*AP*TP*TP*TP*AP*GP*CP*AP*AP*AP*AP*CP*GP*TP*GP*GP*CP*AP*T)-3', 5'-D(P*AP*TP*GP*CP*CP*AP*CP*GP*TP*TP*TP*TP*GP*CP*TP*AP*AP*AP*TP*C)-3', Multiple antibiotic resistance protein marA, ... (4 entities in total) |
Functional Keywords | protein-dna complex, ternary complex, mara, rna polymerase, transcription-dna complex, transcription/dna |
Biological source | Escherichia coli More |
Total number of polymer chains | 4 |
Total formula weight | 37281.43 |
Authors | Dangi, B.,Gronenborn, A.M.,Rosner, J.L.,Martin, R.G. (deposition date: 2004-10-18, release date: 2004-10-26, Last modification date: 2024-05-22) |
Primary citation | Dangi, B.,Gronenborn, A.M.,Rosner, J.L.,Martin, R.G. Versatility of the carboxy-terminal domain of the alpha subunit of RNA polymerase in transcriptional activation: use of the DNA contact site as a protein contact site for MarA. Mol.Microbiol., 54:45-59, 2004 Cited by PubMed Abstract: The transcriptional activator, MarA, interacts with RNA polymerase (RNAP) to activate promoters of the mar regulon. Here, we identify the interacting surfaces of MarA and of the carboxy-terminal domain of the alpha subunit of RNAP (alpha-CTD) by NMR-based chemical shift mapping. Spectral changes were monitored for a MarA-DNA complex upon titration with alpha-CTD, and for alpha-CTD upon titration with MarA-DNA. The mapping results were confirmed by mutational studies and retention chromatography. A model of the ternary complex shows that alpha-CTD uses a '265-like determinant' to contact MarA at a surface distant from the DNA. This is unlike the interaction of alpha-CTD with the CRP or Fis activators where the '265 determinant' contacts DNA while another surface of the same alpha-CTD molecule contacts the activator. These results reveal a new versatility for alpha-CTD in transcriptional activation. PubMed: 15458404DOI: 10.1111/j.1365-2958.2004.04250.x PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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