Stockholms universitet, Institutionen för molekylär biovetenskap, Wenner-Grens institut
Abstract
Endolysins are used by bacteriophages to break down the cell wall of the bacterial host towards the end of the infection cycle. Endolysins are interesting options for the creation of antibacterial substances and domains from endolysins can be combined with domains from other proteins to create antibacterial constructs. This article aims to find the tertiary structure and the enzymatically active site of the endolysin SU57e. This is done through the use of bioinformatics software, comparative analysis with other endolysins, and attempts at producing and purifying the protein for crystallization. SU57e is encoded by the phage vB_EcoD_SU57 (SU57) previously characterized by Koonjan et al. Bioinformatics analysis indicates that the structure is similar to that of endolysin R21 presented by Sun et al. SU57e also appears to have a signal-anchor-release-domain similar to that of R21.