[English] 日本語

- EMDB-21967: Cryo-EM structure of the GltPh L152C-G321C mutant in the intermed... -
+
Open data
-
Basic information
Entry | Database: EMDB / ID: EMD-21967 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Cryo-EM structure of the GltPh L152C-G321C mutant in the intermediate chloride conducting state. | |||||||||
![]() | ||||||||||
![]() | Glutamate transporter homolog GltPh monomer in intermediate chloride conducting configuration: Glutamate transporter homolog / ligand ![]() | |||||||||
Function / homology | ![]() 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 / ![]() ![]() ![]() | |||||||||
Biological species | ![]() ![]() ![]() ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Font J / Chen I / Sobti M / Stewart AG / Ryan RM | |||||||||
Funding support | ![]()
| |||||||||
![]() | ![]() 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 | ![]() ![]() ![]() ![]() | |||||||||
History |
|
-
Structure visualization
Movie |
![]() |
---|---|
Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
-
Downloads & links
-
Download
Header (meta data in XML format) |
|
---|---|
Images |
|
![]() |
|
Archive directory |
-Related structure data
Related structure data | ![]() 6wykCM ![]() 6wyjC ![]() 6wylC ![]() 6wzbC ![]() 6x01C C: citing same article ( M: atomic model generated by this map |
---|---|
Similar-shape strucutres |
-
Links
EMDB pages | ![]() ![]() |
---|---|
Related items in Molecule of the Month |
-
Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.986 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
|
-Supplemental data
-
Sample components
-Entire Glutamate transporter homolog GltPh monomer in intermediate chlor...
Entire | Name: Glutamate transporter homolog GltPh monomer in intermediate chloride conducting configuration Number of components: 3 |
---|
-Component #1: protein, Glutamate transporter homolog GltPh monomer in intermedi...
Protein | Name: Glutamate transporter homolog GltPh monomer in intermediate chloride conducting configuration Recombinant expression: No |
---|---|
Source | Species: ![]() ![]() ![]() |
Source (engineered) | Expression System: ![]() ![]() ![]() |
-Component #2: protein, Glutamate transporter homolog
Protein | Name: Glutamate transporter homolog / Number of Copies: 1 / Recombinant expression: No |
---|---|
Mass | Theoretical: 44.585035 kDa |
Source | Species: ![]() ![]() ![]() Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3 |
Source (engineered) | Expression System: ![]() ![]() ![]() |
-Component #3: ligand, ASPARTIC ACID
Ligand | Name: ASPARTIC ACID![]() |
---|---|
Mass | Theoretical: 0.133103 kDa |
-Experimental details
-
Sample preparation
Specimen | Specimen state: Particle / Method: ![]() |
---|---|
Sample solution | pH: 7.5 |
Vitrification | Cryogen name: ETHANE |
-
Electron microscopy imaging
Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
---|---|
![]() | Microscope: FEI TALOS ARCTICA |
Electron gun | Electron source: FIELD EMISSION GUN![]() |
Lens | Imaging mode: BRIGHT FIELD![]() |
Specimen Holder | Model: OTHER |
Camera | Detector: FEI FALCON III (4k x 4k) |
-
Image processing
![]() | Method: ![]() |
---|---|
3D reconstruction | Software: RELION / Resolution: 4 Å / Resolution method: FSC 0.143 CUT-OFF |
-Atomic model buiding
Output model |
---|