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

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

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

Division of Biological and Biomedical Sciences

Research output: Contribution to journal › Article › peer-review

636 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 language	English
Pages (from-to)	929-938
Number of pages	10
Journal	Cell
Volume	80
Issue number	6
DOIs	https://doi.org/10.1016/0092-8674(95)90296-1
State	Published - Mar 24 1995

Funding

We thank Dr. Steve Clark of Amgen, Inc. for augmenting the sequence alignment program MALIGNED v1.65d to run on a DEC ALPHA system, Dr. James Naismith for assistance with data collection and processing, and Drs. J. Rizo, James Clark, and Elizabeth J. Goldsmith for their valuable discussions. This work was supported in part by a Welch Foundation grant 1-1229 (S. R. S) and a grant from the Perot Family Foundation (T. C. S.).

Funder number
1-1229

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10.1016/0092-8674(95)90296-1

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@article{f6a4960229d241c0aeba3612a278b4fd,

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

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 {\AA} 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.",

author = "Sutton, \{R. Bryan\} and Davletov, \{Bazbek A.\} and Berghuis, \{Albert M.\} and Sudhof, \{Thomas C.\} and Sprang, \{Stephen R.\}",

note = "Funding Information: We thank Dr. Steve Clark of Amgen, Inc. for augmenting the sequence alignment program MALIGNED v1.65d to run on a DEC ALPHA system, Dr. James Naismith for assistance with data collection and processing, and Drs. J. Rizo, James Clark, and Elizabeth J. Goldsmith for their valuable discussions. This work was supported in part by a Welch Foundation grant 1-1229 (S. R. S) and a grant from the Perot Family Foundation (T. C. S.).",

year = "1995",

month = mar,

day = "24",

doi = "10.1016/0092-8674(95)90296-1",

language = "English",

volume = "80",

pages = "929--938",

journal = "Cell",

issn = "0092-8674",

publisher = "Elsevier B.V.",

number = "6",

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TY - JOUR

T1 - Structure of the first C2 domain of synaptotagmin I

T2 - A novel Ca2+/phospholipid-binding fold

AU - Sutton, R. Bryan

AU - Davletov, Bazbek A.

AU - Berghuis, Albert M.

AU - Sudhof, Thomas C.

AU - Sprang, Stephen R.

N1 - Funding Information: We thank Dr. Steve Clark of Amgen, Inc. for augmenting the sequence alignment program MALIGNED v1.65d to run on a DEC ALPHA system, Dr. James Naismith for assistance with data collection and processing, and Drs. J. Rizo, James Clark, and Elizabeth J. Goldsmith for their valuable discussions. This work was supported in part by a Welch Foundation grant 1-1229 (S. R. S) and a grant from the Perot Family Foundation (T. C. S.).

PY - 1995/3/24

Y1 - 1995/3/24

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0028986240

U2 - 10.1016/0092-8674(95)90296-1

DO - 10.1016/0092-8674(95)90296-1

M3 - Article

C2 - 7697723

AN - SCOPUS:0028986240

SN - 0092-8674

VL - 80

SP - 929

EP - 938

JO - Cell

JF - Cell

IS - 6

ER -

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

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