3EZ2

Partition protein-ADP complex

3EZ2 の概要

• エントリーDOI: 10.2210/pdb3ez2/pdb
• 関連するPDBエントリー: 3EZ6 3EZ7 3EZ9 3EZF
• 分子名称: Plasmid partition protein A, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: par, partition, type ia, dna binding, winged-hth, dna binding protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 90826.95

構造登録者

Schumacher, M.A.,Dunham, T.D.,Xu, W.,Funnell, B. (登録日: 2008-10-22, 公開日: 2009-06-02, 最終更新日: 2023-09-06)

主引用文献

Dunham, T.D.,Xu, W.,Funnell, B.E.,Schumacher, M.A.
Structural basis for ADP-mediated transcriptional regulation by P1 and P7 ParA.
Embo J., 28:1792-1802, 2009

PubMed Abstract: The accurate segregation of DNA is essential for the faithful inheritance of genetic information. Segregation of the prototypical P1 plasmid par system requires two proteins, ParA and ParB, and a centromere. When bound to ATP, ParA mediates segregation by interacting with centromere-bound ParB, but when bound to ADP, ParA fulfils a different function: DNA-binding transcription autoregulation. The structure of ParA is unknown as is how distinct nucleotides arbitrate its different functions. To address these questions, we carried out structural and biochemical studies. Crystal structures show that ParA consists of an elongated N-terminal alpha-helix, which unexpectedly mediates dimerization, a winged-HTH and a Walker-box containing C-domain. Biochemical data confirm that apoParA forms dimers at physiological concentrations. Comparisons of four apoParA structures reveal a strikingly flexible dimer interface that allows ParA to adopt multiple conformations. The ParA-ADP structure shows that ADP-binding activates DNA binding using a bipartite mechanism. First, it locks in one specific dimer conformation, and second, it induces the folding of two DNA-binding basic motifs that we show are critical for operator binding.

PubMed: 19461582
DOI: 10.1038/emboj.2009.120

実験手法

X-RAY DIFFRACTION (2.05 Å)