Supramolecular structural analysis of the pore forming protein

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To elucidate the pore forming oligomeric structure of the hemolytic lectin derived from sea invertebrate Cucumaria echinata, small-angle x-ray scattering and circular dicolorism(CD) were carried out. CEL-III forms 25-mer in artificial oligomerization solution, but it dissociate into hexamer in the presence of detergent. This suggests that the hexamer is minimum unit of hemolytic activity. Kratky plot showed that the tertiary structure of CEL-III was destroyed and spectra were similar to that of the random coil structure in the absence of Ca^(2+)or lacturose or both. Whereas, CD spectra showed that the secondary structure was almost same as monomeric CEL-III under the same condition. These results suggest that the tertiary structure of CEL-III under the oligomerization was almost destroyed, but still contains same secondary structure as monomeric CEL-III.