GP0.4 from bacteriophage T7: in silico characterisation of its structure and interaction with E. coli FtsZ.

ABSTRACT:

Background

Proteins produced by bacteriophages can have potent antimicrobial activity. The study of phage-host interactions can therefore inform small molecule drug discovery by revealing and characterising new drug targets. Here we characterise in silico the predicted interaction of gene protein 0.4 (GP0.4) from the Escherichia coli (E. coli) phage T7 with E. coli filamenting temperature-sensitive mutant Z division protein (FtsZ). FtsZ is a tubulin homolog which plays a key role in bacterial cell division and that has been proposed as a drug target.

Results

Using ab initio, fragment assembly structure modelling, we predicted the structure of GP0.4 with two programs. A structure similarity-based network was used to identify a U-shaped helix-turn-helix candidate fold as being

SUBMITTER: Simpkin AJ 

PROVIDER: S-EPMC4944311 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature