8sbe
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the rat vesicular glutamate transporter 2 determined by single-particle Cryo-EM== | |
| + | <StructureSection load='8sbe' size='340' side='right'caption='[[8sbe]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8sbe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6v4d 6v4d]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8SBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SBE FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8sbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8sbe OCA], [https://pdbe.org/8sbe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8sbe RCSB], [https://www.ebi.ac.uk/pdbsum/8sbe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8sbe ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/VGLU2_RAT VGLU2_RAT] Mediates the uptake of glutamate into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. May also play a role in the endocrine glutamatergic system of other tissues such as pineal gland and pancreas. May also mediate the transport of inorganic phosphate.<ref>PMID:11502256</ref> <ref>PMID:11551935</ref> <ref>PMID:11698619</ref> <ref>PMID:11698620</ref> <ref>PMID:17046815</ref> <ref>PMID:18080752</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | Ion transport and regulation in a synaptic vesicle glutamate transporter.,Li F, Eriksen J, Finer-Moore J, Chang R, Nguyen P, Bowen A, Myasnikov A, Yu Z, Bulkley D, Cheng Y, Edwards RH, Stroud RM Science. 2020 May 22;368(6493):893-897. doi: 10.1126/science.aba9202. PMID:32439795<ref>PMID:32439795</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8sbe" style="background-color:#fffaf0;"></div> |
| - | [[Category: Cheng | + | == References == |
| - | [[Category: Edwards | + | <references/> |
| - | [[Category: Finer-Moore | + | __TOC__ |
| - | [[Category: Li | + | </StructureSection> |
| - | [[Category: | + | [[Category: Large Structures]] |
| + | [[Category: Rattus norvegicus]] | ||
| + | [[Category: Cheng Y]] | ||
| + | [[Category: Edwards R]] | ||
| + | [[Category: Eriksen J]] | ||
| + | [[Category: Finer-Moore J]] | ||
| + | [[Category: Li F]] | ||
| + | [[Category: Stroud R]] | ||
Current revision
Structure of the rat vesicular glutamate transporter 2 determined by single-particle Cryo-EM
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