1xs9 | pdb_00001xs9
A MODEL OF THE TERNARY COMPLEX FORMED BETWEEN MARA, THE ALPHA-CTD OF RNA POLYMERASE AND DNA
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Overview
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.
About this Structure
1XS9 is a Protein complex structure of sequences from Escherichia coli. This structure superseeds the now removed PDB entry 1TI9. Active as DNA-directed RNA polymerase, with EC number 2.7.7.6 Full crystallographic information is available from OCA.
Reference
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., Dangi B, Gronenborn AM, Rosner JL, Martin RG, Mol Microbiol. 2004 Oct;54(1):45-59. PMID:15458404
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