Structure of the first C2 domain of synaptotagmin I: A novel Ca2+/phospholipid-binding fold

R. Bryan Sutton, Bazbek A. Davletov, Albert M. Berghuis, Thomas C. Sudhof, Stephen R. Sprang

Research output: Contribution to journalArticlepeer-review

625 Scopus citations

Abstract

C2 domains are regulatory sequence motifs that occur widely in nature. Synaptotagmin I, a synaptic vesicle protein involved in the Ca2+ regulation of exocytosis, contains two C2 domains, the first of which acts as a Ca2+ sensor. We now describe the three-dimensional structure of this C2 domain at 1.9 Å resolution in both the Ca2+-bound and Ca2+-free forms. The C2 polypeptide forms an eight-stranded β sandwich constructed around a conserved four-stranded motif designated as a C2 key. Ca2+ binds in a cup-shaped depression between two polypeptide loops located at the N- and C-termini of the C2-key motif.

Original languageEnglish
Pages (from-to)929-938
Number of pages10
JournalCell
Volume80
Issue number6
DOIs
StatePublished - Mar 24 1995

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