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Structure paper

TitleStructural ensemble of a glutamate transporter homologue in lipid nanodisc environment.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 998, Year 2020
Publish dateFeb 21, 2020
AuthorsValentina Arkhipova / Albert Guskov / Dirk J Slotboom /
PubMed AbstractGlutamate transporters are cation-coupled secondary active membrane transporters that clear the neurotransmitter L-glutamate from the synaptic cleft. These transporters are homotrimers, with each ...Glutamate transporters are cation-coupled secondary active membrane transporters that clear the neurotransmitter L-glutamate from the synaptic cleft. These transporters are homotrimers, with each protomer functioning independently by an elevator-type mechanism, in which a mobile transport domain alternates between inward- and outward-oriented states. Using single-particle cryo-EM we have determined five structures of the glutamate transporter homologue Glt, a Na- L-aspartate symporter, embedded in lipid nanodiscs. Dependent on the substrate concentrations used, the protomers of the trimer adopt a variety of asymmetrical conformations, consistent with the independent movement. Six of the 15 resolved protomers are in a hitherto elusive state of the transport cycle in which the inward-facing transporters are loaded with Na ions. These structures explain how substrate-leakage is prevented - a strict requirement for coupled transport. The belt protein of the lipid nanodiscs bends around the inward oriented protomers, suggesting that membrane deformations occur during transport.
External linksNat Commun / PubMed:32081874 / PubMed Central
MethodsEM (single particle)
Resolution3.22 - 3.47 Å
Structure data

10632

6xwn

EMDB-10632, PDB-6xwn:
Structure of glutamate transporter homologue GltTk in the presence of TBOA inhibitor
Method: EM (single particle) / Resolution: 3.47 Å

10633

6xwo

EMDB-10633, PDB-6xwo:
Structure of glutamate transporter homologue GltTk in the unsaturated conditions - inward-inward-outward configuration
Method: EM (single particle) / Resolution: 3.39 Å

10634

6xwp

EMDB-10634, PDB-6xwp:
Structure of glutamate transporter homologue GltTk in unsaturated conditions - outward-outward-inward configuration
Method: EM (single particle) / Resolution: 3.38 Å

10635

6xwq

EMDB-10635, PDB-6xwq:
Structure of glutamate transporter homologue GltTk in the saturated conditions
Method: EM (single particle) / Resolution: 3.41 Å

10636

6xwr

EMDB-10636, PDB-6xwr:
Structure of glutamate transporter homologue GltTk in sodium only condition
Method: EM (single particle) / Resolution: 3.22 Å

Chemicals

ChemComp-TB1:
(3S)-3-(BENZYLOXY)-L-ASPARTIC ACID

ChemComp-ASP:
ASPARTIC ACID / Aspartic acid

Source
  • Thermococcus kodakarensis KOD1 (archaea)
  • thermococcus kodakarensis (strain atcc baa-918 / jcm 12380 / kod1) (archaea)
KeywordsTRANSPORT PROTEIN / AMINO ACID TRANSPORTER / ASPARTATE TRANSPORT / GLUTAMATE TRANSPORTER HOMOLOGUE / MEMBRANE PROTEIN

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