Abstract
CEL-III is a Ca2+-dependent animal lectin from the sea cucumber, Cucumaria echinata, which shows binding specificity for galactose-containing carbohydrates and exhibits hemolytic and hemagglutinating activities. We have determined its crystal structure at 1.7 A resolution by using single isomorphous replacement with anomalous scattering of lead. CEL-III consists of N-terminal two carbohydrate-binding domains and a C-terminal domain, which is essential for oligomerization and binding to a membrane. CEL-III is the first structure with two β-trefoil folds containing five Ca2+ ions. Here, we report the structural features of CEL-III and discuss the mechanisms of recognition of carbohydrates and hemolysis.
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