Structure of the first C₂ domain of synaptotagmin I: A Novel CA(2+)/Phospholipid-Binding Fold

Authors

R. Bryan Sutton, University of Texas Southwestern Medical Center
Bazbek A. Davletov, Howard Hughes Medical Institute
Albert M. Berghuis, University of Texas Southwestern Medical Center
Thomas C. Sudhof, Howard Hughes Medical Institute
Stephen R. Sprang, University of Montana

Document Type

Article

Publication Title

Cell

Publication Date

3-24-1995

Volume

80

Issue

6

Disciplines

Biology | Life Sciences

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.

DOI

https://doi.org/10.1016/0092-8674(95)90296-1

Rights

© 1995 Cell Press

Recommended Citation

Sutton, R. Bryan; Davletov, Bazbek A.; Berghuis, Albert M.; Sudhof, Thomas C.; and Sprang, Stephen R., "Structure of the first C₂ domain of synaptotagmin I: A Novel CA(2+)/Phospholipid-Binding Fold" (1995). Biological Sciences Faculty Publications. 546.
https://scholarworks.umt.edu/biosci_pubs/546