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1XS9

A MODEL OF THE TERNARY COMPLEX FORMED BETWEEN MARA, THE ALPHA-CTD OF RNA POLYMERASE AND DNA

Replaces:  1TI9
Summary for 1XS9
Entry DOI10.2210/pdb1xs9/pdb
Descriptor5'-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 Keywordsprotein-dna complex, ternary complex, mara, rna polymerase, transcription-dna complex, transcription/dna
Biological sourceEscherichia coli
More
Total number of polymer chains4
Total formula weight37281.43
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 citationDangi, 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: 15458404
DOI: 10.1111/j.1365-2958.2004.04250.x
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

226707

數據於2024-10-30公開中

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