3WX4

CRYSTAL STRUCTURE of T4 PHAGE ARN PROTEIN

3WX4 の概要

• エントリーDOI: 10.2210/pdb3wx4/pdb
• 分子名称: Anti-restriction endonuclease (2 entities in total)
• 機能のキーワード: dna mimic, gene regulation, viral protein
• 由来する生物種: Enterobacteria phage T4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11981.58

構造登録者

Ho, C.H.,Wang, H.C.,Ko, T.P.,Wang, A.H.J. (登録日: 2014-07-16, 公開日: 2014-08-20, 最終更新日: 2024-03-20)

主引用文献

Ho, C.H.,Wang, H.C.,Ko, T.P.,Chang, Y.C.,Wang, A.H.J.
The T4 phage DNA mimic protein Arn inhibits the DNA binding activity of the bacterial histone-like protein H-NS
J.Biol.Chem., 289:27046-27054, 2014

PubMed Abstract: The T4 phage protein Arn (Anti restriction nuclease) was identified as an inhibitor of the restriction enzyme McrBC. However, until now its molecular mechanism remained unclear. In the present study we used structural approaches to investigate biological properties of Arn. A structural analysis of Arn revealed that its shape and negative charge distribution are similar to dsDNA, suggesting that this protein could act as a DNA mimic. In a subsequent proteomic analysis, we found that the bacterial histone-like protein H-NS interacts with Arn, implying a new function. An electrophoretic mobility shift assay showed that Arn prevents H-NS from binding to the Escherichia coli hns and T4 p8.1 promoters. In vitro gene expression and electron microscopy analyses also indicated that Arn counteracts the gene-silencing effect of H-NS on a reporter gene. Because McrBC and H-NS both participate in the host defense system, our findings suggest that T4 Arn might knock down these mechanisms using its DNA mimicking properties.

PubMed: 25118281
DOI: 10.1074/jbc.M114.590851

実験手法

X-RAY DIFFRACTION (1.9 Å)