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TitleGlutamate transporters have a chloride channel with two hydrophobic gates.
Journal, issue, pagesNature, Vol. 591, Issue 7849, Page 327-331, Year 2021
Publish dateFeb 17, 2021
AuthorsIchia Chen / Shashank Pant / Qianyi Wu / Rosemary J Cater / Meghna Sobti / Robert J Vandenberg / Alastair G Stewart / Emad Tajkhorshid / Josep Font / Renae M Ryan /
PubMed AbstractGlutamate 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.
External linksNature / PubMed:33597752 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3.45 - 4.0 Å
Structure data

21966

6wyj

EMDB-21966: Cryo-EM structure of the GltPh L152C-G321C mutant in the intermediate state.
PDB-6wyj: Cryo-EM structure of the GltPh L152C-G321C mutant in the intermediate state
Method: EM (single particle) / Resolution: 3.7 Å

21967

6wyk

EMDB-21967, PDB-6wyk:
Cryo-EM structure of the GltPh L152C-G321C mutant in the intermediate chloride conducting state.
Method: EM (single particle) / Resolution: 4.0 Å

21968

6wyl

EMDB-21968, PDB-6wyl:
Cryo-EM structure of GltPh L152C-G351C mutant in the intermediate outward-facing state.
Method: EM (single particle) / Resolution: 3.9 Å

PDB-6wzb:
Crystal structure of the GltPh V216C-G388C mutant cross-linked with divalent mercury
Method: X-RAY DIFFRACTION / Resolution: 3.45 Å

PDB-6x01:
Crystal structure of the GltPh V216C-A391C mutant cross-linked in outward-facing state
Method: X-RAY DIFFRACTION / Resolution: 3.65 Å

Chemicals

ChemComp-ASP:
ASPARTIC ACID

ChemComp-NA:
Unknown entry

ChemComp-HG:
Unknown entry

Source
  • Pyrococcus horikoshii OT3 (archaea)
  • pyrococcus horikoshii (strain atcc 700860 / dsm 12428 / jcm 9974 / nbrc 100139 / ot-3) (archaea)
KeywordsTRANSPORT PROTEIN / Glutamate transporter homolog Gltph / Glutamate transporter homolog

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