3wx4 | pdb_00003wx4

CRYSTAL STRUCTURE of T4 PHAGE ARN PROTEIN

spinqualitylabelsall models 3wx4, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3wx4 is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ARN_BPT4] Strongly inhibits the RgIB endonuclease. Publication Abstract from PubMed 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. The T4 phage DNA mimic protein Arn inhibits the DNA binding activity of the bacterial histone-like protein H-NS.,Ho CH, Wang HC, Ko TP, Chang YC, Wang AH J Biol Chem. 2014 Sep 26;289(39):27046-54. doi: 10.1074/jbc.M114.590851. Epub, 2014 Aug 12. PMID:25118281 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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