Fig. 2: Crystal structure of Zn2+-dependent LmPC-PLC.
a Activity of WT LmPC-PLC (50 nM) towards 100% POPC MLVs (4.5 mM) in the presence of various bivalent cations (50 μM) in 20 mM MES pH 6.5, 150 mM NaCl. Dunnett’s multiple comparisons test was performed, ns: P > 0.05, *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001. n = 3 independent experiments. Data are presented as mean values ± SEM. Source data are provided as a Source Data file. b Content of the asymmetric unit with marked protein termini (W1 for N-terminus and C as C-terminus) and Zn and Fe ions in the active site (violet and brown spheres, respectively). MolA of LmPC-PLC is shown in blue ribbon and molB in gray. c Left: Superposition of LmPC-PLC molA (blue) and molB (gray). The loops that differ between the molA and mol B are marked in green and red, respectively. The loop S2-T9 is not defined in either of the molecules. α-helices are marked with letters A–H, based on the structure of BcPC-PLC24. Right: zoom in into the active sites of molA and molB. Zn and Fe ion binding residues are shown in sticks. A glycerol molecule is bound in the active site of both molecules and is shown in sticks. Zn and Fe ions are shown as violet and brown spheres, respectively.
