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1RH6

Bacteriophage Lambda Excisionase (Xis)-DNA Complex

1RH6 の概要
エントリーDOI10.2210/pdb1rh6/pdb
分子名称5'-D(*CP*TP*AP*TP*GP*TP*AP*GP*TP*CP*TP*GP*TP*TP*G)-3', 5'-D(P*CP*AP*AP*CP*AP*GP*AP*CP*TP*AP*CP*AP*TP*AP*G)-3', Excisionase, ... (4 entities in total)
機能のキーワードprotein-dna complex, dna architectural protein, 'winged'-helix protein, phage excision, site-specific dna recombination, dna binding protein-dna complex, dna binding protein/dna
由来する生物種Enterobacteria phage lambda
タンパク質・核酸の鎖数4
化学式量合計22764.61
構造登録者
Sam, M.D.,Cascio, D.,Johnson, R.C.,Clubb, R.T. (登録日: 2003-11-13, 公開日: 2004-06-29, 最終更新日: 2024-02-14)
主引用文献Sam, M.D.,Cascio, D.,Johnson, R.C.,Clubb, R.T.
Crystal structure of the excisionase-DNA complex from bacteriophage lambda.
J.Mol.Biol., 338:229-240, 2004
Cited by
PubMed Abstract: The excisionase (Xis) protein from bacteriophage lambda is the best characterized member of a large family of recombination directionality factors that control integrase-mediated DNA rearrangements. It triggers phage excision by cooperatively binding to sites X1 and X2 within the phage, bending DNA significantly and recruiting the phage-encoded integrase (Int) protein to site P2. We have determined the co-crystal structure of Xis with its X2 DNA-binding site at 1.7A resolution. Xis forms a unique winged-helix motif that interacts with the major and minor grooves of its binding site using an alpha-helix and an ordered beta-hairpin (wing), respectively. Recognition is achieved through an elaborate water-mediated hydrogen-bonding network at the major groove interface, while the preformed hairpin forms largely non-specific interactions with the minor groove. The structure of the complex provides insights into how Xis recruits Int cooperatively, and suggests a plausible mechanism by which it may distort longer DNA fragments significantly. It reveals a surface on the protein that is likely to mediate Xis-Xis interactions required for its cooperative binding to DNA.
PubMed: 15066428
DOI: 10.1016/j.jmb.2004.02.053
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.7 Å)
構造検証レポート
Validation report summary of 1rh6
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-13に公開中

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