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PDBsum entry 2yoa
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Signaling protein
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PDB id
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2yoa
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PDB id:
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| Name: |
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Signaling protein
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Title:
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Synaptotagmin-1 c2b domain with phosphoserine
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Structure:
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Synaptotagmin-1. Chain: a, b. Fragment: c2b domain, residues 271-421. Synonym: synaptotagmin i, syti, p65. Engineered: yes
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Source:
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Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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1.50Å
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R-factor:
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0.184
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R-free:
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0.204
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Authors:
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A.Honigmann,G.Van Den Bogaart,E.Iraheta,H.J.Risselada,D.Milovanovic, V.Mueller,S.Muellar,U.Diederichsen,D.Fasshauer,H.Grubmuller, S.W.Hell,C.Eggeling,K.Kuhnel,R.Jahn
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Key ref:
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A.Honigmann
et al.
(2013).
Phosphatidylinositol 4,5-bisphosphate clusters act as molecular beacons for vesicle recruitment.
Nat Struct Biol,
20,
679-686.
PubMed id:
DOI:
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Date:
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22-Oct-12
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Release date:
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20-Mar-13
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PROCHECK
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Headers
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References
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P21707
(SYT1_RAT) -
Synaptotagmin-1 from Rattus norvegicus
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Seq:
Struc:
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421 a.a.
149 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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Nat Struct Biol
20:679-686
(2013)
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PubMed id:
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Phosphatidylinositol 4,5-bisphosphate clusters act as molecular beacons for vesicle recruitment.
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A.Honigmann,
G.van den Bogaart,
E.Iraheta,
H.J.Risselada,
D.Milovanovic,
V.Mueller,
S.Müllar,
U.Diederichsen,
D.Fasshauer,
H.Grubmüller,
S.W.Hell,
C.Eggeling,
K.Kühnel,
R.Jahn.
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ABSTRACT
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Synaptic-vesicle exocytosis is mediated by the vesicular Ca(2+) sensor
synaptotagmin-1. Synaptotagmin-1 interacts with the SNARE protein syntaxin-1A
and acidic phospholipids such as phosphatidylinositol 4,5-bisphosphate (PIP2).
However, it is unclear how these interactions contribute to triggering membrane
fusion. Using PC12 cells from Rattus norvegicus and artificial supported
bilayers, we show that synaptotagmin-1 interacts with the polybasic linker
region of syntaxin-1A independent of Ca(2+) through PIP2. This interaction
allows both Ca(2+)-binding sites of synaptotagmin-1 to bind to
phosphatidylserine in the vesicle membrane upon Ca(2+) triggering. We determined
the crystal structure of the C2B domain of synaptotagmin-1 bound to
phosphoserine, allowing development of a high-resolution model of synaptotagmin
bridging two different membranes. Our results suggest that PIP2 clusters
organized by syntaxin-1 act as molecular beacons for vesicle docking, with the
subsequent Ca(2+) influx bringing the vesicle membrane close enough for membrane
fusion.
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Links
