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Structure paper

TitleLarge domain movements through the lipid bilayer mediate substrate release and inhibition of glutamate transporters.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateNov 6, 2020
AuthorsXiaoyu Wang / Olga Boudker /
PubMed AbstractGlutamate 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.
External linksElife / PubMed:33155546 / PubMed Central
MethodsEM (single particle)
Resolution3.05 - 3.71 Å
Structure data

21986

6x12

EMDB-21986, PDB-6x12:
Inward-facing Apo-open state of the glutamate transporter homologue GltPh
Method: EM (single particle) / Resolution: 3.52 Å

21987

6x13

EMDB-21987, PDB-6x13:
Inward-facing sodium-bound state of the glutamate transporter homologue GltPh
Method: EM (single particle) / Resolution: 3.66 Å

21988

6x14

EMDB-21988, PDB-6x14:
Inward-facing state of the glutamate transporter homologue GltPh in complex with TFB-TBOA
Method: EM (single particle) / Resolution: 3.71 Å

21989

6x15

EMDB-21989, PDB-6x15:
Inward-facing state of the glutamate transporter homologue GltPh in complex with L-aspartate and sodium ions
Method: EM (single particle) / Resolution: 3.05 Å

21990

6x16

EMDB-21990, PDB-6x16:
Inward-facing state of the glutamate transporter homologue GltPh in complex with TBOA
Method: EM (single particle) / Resolution: 3.39 Å

21991

6x17

EMDB-21991, PDB-6x17:
Outward-facing state of the glutamate transporter homologue GltPh in complex with TBOA
Method: EM (single particle) / Resolution: 3.66 Å

Chemicals

ChemComp-6OU:
[(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate / phospholipid*YM

ChemComp-7O9:
(2~{S},3~{S})-2-azanyl-3-[[3-[[4-(trifluoromethyl)phenyl]carbonylamino]phenyl]methoxy]butanedioic acid

ChemComp-NA:
Unknown entry

ChemComp-ASP:
ASPARTIC ACID / Aspartic acid

ChemComp-HG:
Unknown entry / Mercury (element)

ChemComp-HOH:
WATER / Water

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

Source
  • pyrococcus horikoshii (archaea)
KeywordsTRANSPORT PROTEIN / sodium-coupled L-aspartate transporter

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