3FDQ

Recognition of AT-rich DNA binding sites by the MogR Repressor

Summary for 3FDQ

• Entry DOI: 10.2210/pdb3fdq/pdb
• Descriptor: Motility gene repressor mogR, 5'-D(*AP*TP*TP*TP*TP*TP*TP*AP*AP*AP*AP*AP*AP*AP*T)-3', 5'-D(*TP*AP*TP*TP*TP*TP*TP*TP*TP*AP*AP*AP*AP*AP*A)-3', ... (4 entities in total)
• Functional Keywords: protein-dna complex, helix-turn-helix, minor groove binding, cytoplasm, dna-binding, repressor, transcription, transcription regulation, virulence, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Listeria monocytogenes; More
• Cellular location: Cytoplasm: Q8Y960
• Total number of polymer chains: 4
• Total formula weight: 48818.77

Authors

Shen, A.,Higgins, D.E.,Panne, D. (deposition date: 2008-11-26, release date: 2009-06-02, Last modification date: 2023-12-27)

Primary citation

Shen, A.,Higgins, D.E.,Panne, D.
Recognition of AT-Rich DNA Binding Sites by the MogR Repressor.
Structure, 17:769-777, 2009

PubMed Abstract: The MogR transcriptional repressor of the intracellular pathogen Listeria monocytogenes recognizes AT-rich binding sites in promoters of flagellar genes to downregulate flagellar gene expression during infection. We describe here the 1.8 A resolution crystal structure of MogR bound to the recognition sequence 5' ATTTTTTAAAAAAAT 3' present within the flaA promoter region. Our structure shows that MogR binds as a dimer. Each half-site is recognized in the major groove by a helix-turn-helix motif and in the minor groove by a loop from the symmetry-related molecule, resulting in a "crossover" binding mode. This oversampling through minor groove interactions is important for specificity. The MogR binding site has structural features of A-tract DNA and is bent by approximately 52 degrees away from the dimer. The structure explains how MogR achieves binding specificity in the AT-rich genome of L. monocytogenes and explains the evolutionary conservation of A-tract sequence elements within promoter regions of MogR-regulated flagellar genes.

PubMed: 19446532
DOI: 10.1016/j.str.2009.02.018

Experimental method

X-RAY DIFFRACTION (1.75 Å)