1RSY

STRUCTURE OF THE FIRST C2-DOMAIN OF SYNAPTOTAGMIN I: A NOVEL CA2+(SLASH)PHOSPHOLIPID BINDING FOLD

Summary for 1RSY

• Entry DOI: 10.2210/pdb1rsy/pdb
• Descriptor: SYNAPTOTAGMIN I, SULFATE ION (3 entities in total)
• Functional Keywords: calcium/phospholipid binding protein, calcium-phospholipid binding protein complex
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass membrane protein: P21707
• Total number of polymer chains: 1
• Total formula weight: 17194.41

Authors

Sutton, R.B.,Sprang, S.R. (deposition date: 1995-02-01, release date: 1995-05-08, Last modification date: 2024-02-14)

Primary citation

Sutton, R.B.,Davletov, B.A.,Berghuis, A.M.,Sudhof, T.C.,Sprang, S.R.
Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold.
Cell(Cambridge,Mass.), 80:929-938, 1995

PubMed 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 A resolution in both the Ca(2+)-bound and Ca(2+)-free forms. The C2 polypeptide forms an eight-stranded beta 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.

PubMed: 7697723
DOI: 10.1016/0092-8674(95)90296-1

Experimental method

X-RAY DIFFRACTION (1.9 Å)