|Entry||Database: PDB / ID: 6x12|
|Title||Inward-facing Apo-open state of the glutamate transporter homologue GltPh|
|Components||Glutamate transporter homologue GltPh|
|Keywords||TRANSPORT PROTEIN / sodium-coupled L-aspartate transporter|
|Biological species||Pyrococcus horikoshii (archaea)|
|Method||ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.52 Å|
|Authors||Wang, X. / Boudker, O.|
|Funding support|| United States, 2items |
|Citation||Journal: Elife / Year: 2020|
Title: Large domain movements through the lipid bilayer mediate substrate release and inhibition of glutamate transporters.
Authors: Xiaoyu Wang / Olga Boudker /
Abstract: Glutamate transporters are essential players in glutamatergic neurotransmission in the brain, where they maintain extracellular glutamate below cytotoxic levels and allow for rounds of transmission. ...Glutamate transporters are essential players in glutamatergic neurotransmission in the brain, where they maintain extracellular glutamate below cytotoxic levels and allow for rounds of transmission. The structural bases of their function are well established, particularly within a model archaeal homolog, sodium, and aspartate symporter Glt. However, the mechanism of gating on the cytoplasmic side of the membrane remains ambiguous. We report Cryo-EM structures of Glt reconstituted into nanodiscs, including those structurally constrained in the cytoplasm-facing state and either apo, bound to sodium ions only, substrate, or blockers. The structures show that both substrate translocation and release involve movements of the bulky transport domain through the lipid bilayer. They further reveal a novel mode of inhibitor binding and show how solutes release is coupled to protein conformational changes. Finally, we describe how domain movements are associated with the displacement of bound lipids and significant membrane deformations, highlighting the potential regulatory role of the bilayer.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
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A: Glutamate transporter homologue GltPh
|#1: Protein|| |
Mass: 44643.918 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pyrococcus horikoshii (archaea) / Production host: Escherichia coli (E. coli)
|#2: Chemical|| ChemComp-6OU / [(|
|Has ligand of interest||N|
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction|
|Component||Name: Complex of inward-facing Apo-open state of GltPh in MSP1E3 nanodisc|
Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT
|Molecular weight||Value: 0.134 MDa / Experimental value: NO|
|Source (natural)||Organism: Pyrococcus horikoshii (archaea)|
|Source (recombinant)||Organism: Escherichia coli (E. coli)|
|Buffer solution||pH: 7.4|
|Specimen||Embedding applied: YES / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Specimen support||Details: unspecified|
|EM embedding||Material: ice|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Microscopy||Model: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELDBright-field microscopy|
|Image recording||Electron dose: 68.55 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Symmetry||Point symmetry: C1 (asymmetric)|
|3D reconstruction||Resolution: 3.52 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 148582 / Symmetry type: POINT|
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