Fig. 3: Structural and functional comparison of LmPC-PLC with the bacterial homologs.
a Left: Superposition of all three bacterial PC-PLC homologs (BcPC-PLC: PDB-ID 1 AH7, orange ribbons; CpPC-PLC: PDB-ID 1CA1, green ribbons; LmPC-PLC molB, gray ribbons. Right: Zoom in into the active sites of the three homologs. Zn ions are shown as spheres in the same colors as ribbons in Bc- and CpPC-PLC, except for violet for Zn and brown for Fe in LmPC-PLC, and numbered. Zn/Fe ion coordinating residues are shown in sticks and labeled. In CpPC-PLC, metal ion positions 1 and 2 are occupied by Cd ions that were present in the crystallization buffer. b Enzymatic activity of LmPC-PLC WT and D55N mutant (500 nM) towards 4-NPPC (1 mM). c Activity of PC-PLC homologs (50 nM) towards 100% POPC MLVs (4.5 mM). d Activity of PC-PLC homologs (500 nM) towards 4-NPPC (1 mM). Experiments in b, c and d were performed in 20 mM MES pH 6.5, 150 mM NaCl, 50 (c) or 500 (b, d) μM ZnSO4, and 1 mM CaCl2 (only for Cp) at 37 °C. Dunnett’s multiple comparisons test (c, d) or Student’s t-test (b) was performed, ns: P > 0.05, *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001. Source data are provided as a Source Data file. n = 3 independent experiments (b–d). Data in (b–d) are presented as mean values ± SEM.
