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PDBsum entry 5cci
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Endocytosis,exocytosis
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PDB id
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5cci
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Contents |
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62 a.a.
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67 a.a.
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73 a.a.
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64 a.a.
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280 a.a.
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PDB id:
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| Name: |
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Endocytosis,exocytosis
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Title:
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Structure of the mg2+-bound synaptotagmin-1 snare complex (short unit cell form)
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Structure:
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Vesicle-associated membrane protein 2. Chain: a. Fragment: unp residues 28-89. Synonym: vamp-2,synaptobrevin-2. Engineered: yes. Syntaxin-1a. Chain: b. Fragment: unp residues 191-256. Synonym: neuron-specific antigen hpc-1,synaptotagmin-associated 35
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Source:
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Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: vamp2, syb2. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: stx1a, sap. Gene: snap25, snap. Gene: syt1.
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Resolution:
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4.10Å
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R-factor:
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0.279
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R-free:
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0.323
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Authors:
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Q.Zhou,M.Zhao,A.Y.Lyubimov,M.Uervirojnangkoorn,W.I.Weis,A.T.Brunger
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Key ref:
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Q.Zhou
et al.
(2015).
Architecture of the synaptotagmin-SNARE machinery for neuronal exocytosis.
Nature,
525,
62-67.
PubMed id:
DOI:
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Date:
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02-Jul-15
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Release date:
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12-Aug-15
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PROCHECK
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Headers
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References
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P63045
(VAMP2_RAT) -
Vesicle-associated membrane protein 2 from Rattus norvegicus
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Seq:
Struc:
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116 a.a.
62 a.a.
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P32851
(STX1A_RAT) -
Syntaxin-1A from Rattus norvegicus
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Seq:
Struc:
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288 a.a.
67 a.a.*
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P60881
(SNP25_RAT) -
Synaptosomal-associated protein 25 from Rattus norvegicus
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Seq:
Struc:
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206 a.a.
73 a.a.*
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DOI no:
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Nature
525:62-67
(2015)
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PubMed id:
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Architecture of the synaptotagmin-SNARE machinery for neuronal exocytosis.
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Q.Zhou,
Y.Lai,
T.Bacaj,
M.Zhao,
A.Y.Lyubimov,
M.Uervirojnangkoorn,
O.B.Zeldin,
A.S.Brewster,
N.K.Sauter,
A.E.Cohen,
S.M.Soltis,
R.Alonso-Mori,
M.Chollet,
H.T.Lemke,
R.A.Pfuetzner,
U.B.Choi,
W.I.Weis,
J.Diao,
T.C.Südhof,
A.T.Brunger.
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ABSTRACT
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Synaptotagmin-1 and neuronal SNARE proteins have central roles in evoked
synchronous neurotransmitter release; however, it is unknown how they cooperate
to trigger synaptic vesicle fusion. Here we report atomic-resolution crystal
structures of Ca(2+)- and Mg(2+)-bound complexes between synaptotagmin-1 and the
neuronal SNARE complex, one of which was determined with diffraction data from
an X-ray free-electron laser, leading to an atomic-resolution structure with
accurate rotamer assignments for many side chains. The structures reveal several
interfaces, including a large, specific, Ca(2+)-independent and conserved
interface. Tests of this interface by mutagenesis suggest that it is essential
for Ca(2+)-triggered neurotransmitter release in mouse hippocampal neuronal
synapses and for Ca(2+)-triggered vesicle fusion in a reconstituted system. We
propose that this interface forms before Ca(2+) triggering, moves en bloc as
Ca(2+) influx promotes the interactions between synaptotagmin-1 and the plasma
membrane, and consequently remodels the membrane to promote fusion, possibly in
conjunction with other interfaces.
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