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. 2021 Jul 15;13(7):1377. doi: 10.3390/v13071377

Figure 1.

Figure 1

In silico analysis of LysB proteins. (a) Modular structure of KZ144 and representative mycobacteriophage’s LysB proteins. Regions with structural similarity to the KZ144 PGBD are shown in light grey blocks and a predicted catalytic region similar to D29 LysB in dark grey. φKZ gp144 lytic transglycosylase domain is marked with a strip pattern. The predicted PGBD in Fruitloop_gp30 is marked with a dot pattern. Each phage cluster is indicated by the letters on the left. The data shown are the result of a HHpred analysis for each depicted mycobacteriophage LysB. Predicted cutinase domains with MOTIF Finder are indicated within the LysBs catalytic region. (b) Alignment between the N-terminus of Ms6 LysB and the PGBD of φKZ endolysin as obtained from HHPred. (c) Structural model of Ms6 LysB using KZ144 (PDB ID-3BKH) as the template obtained from the SWISS-MODEL server. Catalytic and N-terminal domains of KZ144 are represented in light and dark blue, respectively. The generated structure of the N-terminal sequence of Ms6 LysB is represented in red. The sequences with lower similarity with target (low scored) are indicated by an arrow. Image was created with UCSF Chimera [44] and by superposing the PDB structure 3BKH and the constructed Ms6 LysB model.