1LX8

Regulation of directionality in bacteriophage lambda site-specific recombination: structure of the Xis protein

1LX8 の概要

• エントリーDOI: 10.2210/pdb1lx8/pdb
• 分子名称: Excisionase (1 entity in total)
• 機能のキーワード: dna architectural protein, 'winged'-helix protein, phage excision, site-specific dna recombination, viral protein
• 由来する生物種: Enterobacteria phage lambda
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6793.80

構造登録者

Sam, M.D.,Papagiannis, C.,Connolly, K.M.,Corselli, L.,Iwahara, J.,Lee, J.,Phillips, M.,Wojciak, J.M.,Johnson, R.C.,Clubb, R.T. (登録日: 2002-06-04, 公開日: 2003-06-10, 最終更新日: 2024-05-22)

主引用文献

Sam, M.D.,Papagiannis, C.,Connolly, K.M.,Corselli, L.,Iwahara, J.,Lee, J.,Phillips, M.,Wojciak, J.M.,Johnson, R.C.,Clubb, R.T.
Regulation of directionality in bacteriophage lambda site-specific recombination: structure of the Xis protein
J.Mol.Biol., 324:791-805, 2002

PubMed Abstract: Upon induction of a bacteriophage lambda lysogen, a site-specific recombination reaction excises the phage genome from the chromosome of its bacterial host. A critical regulator of this process is the phage-encoded excisionase (Xis) protein, which functions both as a DNA architectural factor and by cooperatively recruiting integrase to an adjacent binding site specifically required for excision. Here we present the three-dimensional structure of Xis and the results of a structure-based mutagenesis study to define the molecular basis of its function. Xis adopts an unusual "winged"-helix motif that is modeled to interact with the major- and minor-grooves of its binding site through a single alpha-helix and loop structure ("wing"), respectively. The C-terminal tail of Xis, which is required for cooperative binding with integrase, is unstructured in the absence of DNA. We propose that asymmetric bending of DNA by Xis positions its unstructured C-terminal tail for direct contacts with the N-terminal DNA-binding domain of integrase and that an ensuing disordered to ordered transition of the tail may act to stabilize the formation of the tripartite integrase-Xis-DNA complex required for phage excision.

PubMed: 12460578
DOI: 10.1016/S0022-2836(02)01150-6

実験手法

SOLUTION NMR