8SBE
Structure of the rat vesicular glutamate transporter 2 determined by single-particle Cryo-EM
Replaces: 6V4DSummary for 8SBE
| Entry DOI | 10.2210/pdb8sbe/pdb |
| EMDB information | 21040 |
| Descriptor | Vesicular glutamate transporter 2 (1 entity in total) |
| Functional Keywords | glutamate transport, synaptic vesicle, major facilitator superfamily, excitatory neurotransmission, membrane protein |
| Biological source | Rattus norvegicus (Norway rat) |
| Total number of polymer chains | 1 |
| Total formula weight | 58893.01 |
| Authors | Li, F.,Finer-Moore, J.,Eriksen, J.,Cheng, Y.,Edwards, R.,Stroud, R. (deposition date: 2023-04-03, release date: 2023-05-03, Last modification date: 2024-06-19) |
| Primary citation | Li, F.,Eriksen, J.,Finer-Moore, J.,Chang, R.,Nguyen, P.,Bowen, A.,Myasnikov, A.,Yu, Z.,Bulkley, D.,Cheng, Y.,Edwards, R.H.,Stroud, R.M. Ion transport and regulation in a synaptic vesicle glutamate transporter. Science, 368:893-897, 2020 Cited by PubMed Abstract: 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. PubMed: 32439795DOI: 10.1126/science.aba9202 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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