Abstract
C 2 domains are regulatory sequence motifs that occur widely in nature. Synaptotagmin I, a synaptic vesicle protein involved in the Ca 2+ regulation of exocytosis, contains two C 2 domains, the first of which acts as a Ca 2+ sensor. We now describe the three-dimensional structure of this C 2 domain at 1.9 Å resolution in both the Ca 2+-bound and Ca 2+-free forms. The C 2 polypeptide forms an eight-stranded β sandwich constructed around a conserved four-stranded motif designated as a C 2 key. Ca 2+ binds in a cup-shaped depression between two polypeptide loops located at the N- and C-termini of the C 2-key motif.
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