|Entry||Database: EMDB / ID: EMD-21968|
|Title||Cryo-EM structure of GltPh L152C-G351C mutant in the intermediate outward-facing state.|
|Sample||Glutamate transporter homolog, GltPh, in nanodisc:|
Glutamate transporter homolog / ligand
|Function / homology|
Function and homology information
amino acid:sodium symporter activity / L-aspartate transmembrane transport / L-aspartate import across plasma membrane / L-aspartate transmembrane transporter activity / chloride transmembrane transporter activity / chloride transmembrane transport / protein homotrimerization / integral component of membrane / identical protein binding / plasma membrane / metal ion binding
Sodium:dicarboxylate symporter, conserved site / Sodium:dicarboxylate symporter / Sodium:dicarboxylate symporter superfamily
Glutamate transporter homolog
|Biological species||Pyrococcus horikoshii OT3 (archaea) / Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (archaea)|
|Method||single particle reconstruction / cryo EM / Resolution: 3.9 Å|
|Authors||Font J / Chen I / Sobti M / Stewart AG / Ryan RM|
|Funding support|| Australia, 1 items |
|Citation||Journal: Nature / Year: 2021|
Title: Glutamate transporters have a chloride channel with two hydrophobic gates.
Authors: Ichia Chen / Shashank Pant / Qianyi Wu / Rosemary J Cater / Meghna Sobti / Robert J Vandenberg / Alastair G Stewart / Emad Tajkhorshid / Josep Font / Renae M Ryan /
Abstract: Glutamate is the most abundant excitatory neurotransmitter in the central nervous system, and its precise control is vital to maintain normal brain function and to prevent excitotoxicity. The removal ...Glutamate is the most abundant excitatory neurotransmitter in the central nervous system, and its precise control is vital to maintain normal brain function and to prevent excitotoxicity. The removal of extracellular glutamate is achieved by plasma-membrane-bound transporters, which couple glutamate transport to sodium, potassium and pH gradients using an elevator mechanism. Glutamate transporters also conduct chloride ions by means of a channel-like process that is thermodynamically uncoupled from transport. However, the molecular mechanisms that enable these dual-function transporters to carry out two seemingly contradictory roles are unknown. Here we report the cryo-electron microscopy structure of a glutamate transporter homologue in an open-channel state, which reveals an aqueous cavity that is formed during the glutamate transport cycle. The functional properties of this cavity, combined with molecular dynamics simulations, reveal it to be an aqueous-accessible chloride permeation pathway that is gated by two hydrophobic regions and is conserved across mammalian and archaeal glutamate transporters. Our findings provide insight into the mechanism by which glutamate transporters support their dual function, and add information that will assist in mapping the complete transport cycle shared by the solute carrier 1A transporter family.
|Validation Report||Summary, Full report, XML, About validation report|
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_21968.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 0.986 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire Glutamate transporter homolog, GltPh, in nanodisc
|Entire||Name: Glutamate transporter homolog, GltPh, in nanodisc / Number of components: 3|
-Component #1: protein, Glutamate transporter homolog, GltPh, in nanodisc
|Protein||Name: Glutamate transporter homolog, GltPh, in nanodisc / Recombinant expression: No|
|Source||Species: Pyrococcus horikoshii OT3 (archaea)|
|Source (engineered)||Expression System: Escherichia coli (E. coli)|
-Component #2: protein, Glutamate transporter homolog
|Protein||Name: Glutamate transporter homolog / Number of Copies: 3 / Recombinant expression: No|
|Mass||Theoretical: 44.585035 kDa|
|Source||Species: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (archaea)|
Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3
|Source (engineered)||Expression System: Escherichia coli (E. coli)|
-Component #3: ligand, ASPARTIC ACID
|Ligand||Name: ASPARTIC ACID / Number of Copies: 3 / Recombinant expression: No|
|Mass||Theoretical: 0.133103 kDa|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||pH: 7.5|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Talos Arctica / Image courtesy: FEI Company
|Imaging||Microscope: FEI TALOS ARCTICA|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Electron dose: 40 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: FEI FALCON III (4k x 4k)|
|Processing||Method: single particle reconstruction / Applied symmetry: C3 (3 fold cyclic) / Number of projections: 220938|
|3D reconstruction||Software: RELION / Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF|
-Atomic model buiding
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