Figure 1.
ClyF contains an active calcium-binding motif. (a) Alignment of the calcium-binding motif of ClyF with that of LysGH15. Alignment was generated by Clustal Omega and visualized by ESPript. The calcium-binding residues (conserved positions 1, 3, 5, 7 and 12) are indicated by asterisks. (b and c) Bacteriolytic activity of Pc and ClyF (50 mg/L) against S. aureus N315 under various conditions. 1 mM EDTA, 2 mM CaCl2 and MgCl2 were used. (d) The effects of different ions on ClyF activity. ClyF was inactivated by 3 mM EDTA and dialysed against PBS; residual enzymatic activity was then tested against S. aureus N315 in the presence of 4 mM CaCl2, ZnCl2 or MgCl2. ***, Pā€Š<ā€Š0.001. This figure appears in colour in the online version of JAC and in black and white in the print version of JAC.

ClyF contains an active calcium-binding motif. (a) Alignment of the calcium-binding motif of ClyF with that of LysGH15. Alignment was generated by Clustal Omega and visualized by ESPript. The calcium-binding residues (conserved positions 1, 3, 5, 7 and 12) are indicated by asterisks. (b and c) Bacteriolytic activity of Pc and ClyF (50 mg/L) against S. aureus N315 under various conditions. 1 mM EDTA, 2 mM CaCl2 and MgCl2 were used. (d) The effects of different ions on ClyF activity. ClyF was inactivated by 3 mM EDTA and dialysed against PBS; residual enzymatic activity was then tested against S. aureus N315 in the presence of 4 mM CaCl2, ZnCl2 or MgCl2. ***, Pā€Š<ā€Š0.001. This figure appears in colour in the online version of JAC and in black and white in the print version of JAC.

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