3FDQ

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

3FDQ の概要

• エントリーDOI: 10.2210/pdb3fdq/pdb
• 分子名称: 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)
• 機能のキーワード: 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
• 由来する生物種: Listeria monocytogenes; 詳細
• 細胞内の位置: Cytoplasm: Q8Y960
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 48818.77

構造登録者

Shen, A.,Higgins, D.E.,Panne, D. (登録日: 2008-11-26, 公開日: 2009-06-02, 最終更新日: 2023-12-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.75 Å)