2IIE

single chain Integration Host Factor protein (scIHF2) in complex with DNA

2IIE の概要

• エントリーDOI: 10.2210/pdb2iie/pdb
• 関連するPDBエントリー: 1IHF 2IIF
• 分子名称: Phage P H' site, DNA (5'-D(*DGP*DGP*DCP*DCP*DAP*DAP*DAP*DAP*DAP*DAP*DGP*DCP*DAP*DTP*DT)-3'), DNA (5'-D(*DGP*DCP*DTP*DTP*DAP*DTP*DCP*DAP*DAP*DTP*DTP*DTP*DGP*DTP*DTP*DGP*DCP*DAP*DCP*DC)-3'), ... (6 entities in total)
• 機能のキーワード: dna kinking, bending, u-turn, intercalation, divalent, recombination-dna complex, recombination/dna
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm: P0A6Y1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 44757.39

構造登録者

Bao, Q.,Droege, P.,Davey, C.A. (登録日: 2006-09-28, 公開日: 2007-02-20, 最終更新日: 2023-10-25)

主引用文献

Bao, Q.,Chen, H.,Liu, Y.,Yan, J.,Droge, P.,Davey, C.A.
A Divalent Metal-mediated Switch Controlling Protein-induced DNA Bending
J.Mol.Biol., 367:731-740, 2007

PubMed Abstract: Architectural proteins that reconfigure the paths of DNA segments are required for the establishment of functional interfaces in many genomic transactions. A single-chain derivative of the DNA architectural protein integration host factor was found to adopt two stable conformational states in complex with a specific DNA target. In the so-called open state, the degree of protein-induced DNA bending is reduced significantly compared with the closed state. The conformational switch between these states is controlled by divalent metal binding in two electronegative zones arising from the lysine-to-glutamate substitution in the protein body proximal to the phosphate backbone of one DNA arm. We show that this switch can be employed to control the efficiency of site-specific recombination catalyzed by lambda integrase. Introduction of acidic residues at the protein-DNA interface holds potential for the design of metal-mediated switches for the investigation of functional relationships.

PubMed: 17276457
DOI: 10.1016/j.jmb.2006.09.082

実験手法

X-RAY DIFFRACTION (2.41 Å)