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PDBsum entry 8sbe
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Membrane protein
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PDB id
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8sbe
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PDB id:
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| Name: |
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Membrane protein
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Title:
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Structure of the rat vesicular glutamate transporter 2 determined by single-particle cryo-em
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Structure:
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Vesicular glutamate transporter 2. Chain: a. Synonym: vglut2,differentiation-associated bnpi,differentiation- associated na(+)-dependent inorganic phosphate cotransporter,solute carrier family 17 member 6. Engineered: yes. Other_details: synonyms: vglut2, differentiation-associated bnpi, solute carrier family 17 member 6, differentiation-associated na(+)- dependent inorganic phosphate cotransporter
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Source:
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Rattus norvegicus. Norway rat. Organism_taxid: 10116. Gene: slc17a6, dnpi, vglut2. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108
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Authors:
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F.Li,J.Finer-Moore,J.Eriksen,Y.Cheng,R.Edwards,R.Stroud
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Key ref:
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F.Li
et al.
(2020).
Ion transport and regulation in a synaptic vesicle glutamate transporter.
Science,
368,
893-897.
PubMed id:
DOI:
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Date:
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03-Apr-23
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Release date:
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03-May-23
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Supersedes:
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PROCHECK
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Headers
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References
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Q9JI12
(VGLU2_RAT) -
Vesicular glutamate transporter 2 from Rattus norvegicus
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Seq:
Struc:
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582 a.a.
422 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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DOI no:
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Science
368:893-897
(2020)
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PubMed id:
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Ion transport and regulation in a synaptic vesicle glutamate transporter.
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F.Li,
J.Eriksen,
J.Finer-Moore,
R.Chang,
P.Nguyen,
A.Bowen,
A.Myasnikov,
Z.Yu,
D.Bulkley,
Y.Cheng,
R.H.Edwards,
R.M.Stroud.
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ABSTRACT
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Synaptic vesicles accumulate neurotransmitters, enabling the quantal release by
exocytosis that underlies synaptic transmission. Specific neurotransmitter
transporters are responsible for this activity and therefore are essential for
brain function. The vesicular glutamate transporters (VGLUTs) concentrate the
principal excitatory neurotransmitter glutamate into synaptic vesicles, driven
by membrane potential. However, the mechanism by which they do so remains poorly
understood owing to a lack of structural information. We report the
cryo-electron microscopy structure of rat VGLUT2 at 3.8-angstrom resolution and
propose structure-based mechanisms for substrate recognition and allosteric
activation by low pH and chloride. A potential permeation pathway for chloride
intersects with the glutamate binding site. These results demonstrate how the
activity of VGLUTs can be coordinated with large shifts in proton and chloride
concentrations during the synaptic vesicle cycle to ensure normal synaptic
transmission.
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