6XWP

Structure of glutamate transporter homologue GltTk in unsaturated conditions - outward-outward-inward configuration

6XWP の概要

• エントリーDOI: 10.2210/pdb6xwp/pdb
• 関連するPDBエントリー: 6XWN 6XWO 6XWQ 6XWR
• EMDBエントリー: 10634
• 分子名称: Proton/glutamate symporter, SDF family, ASPARTIC ACID (2 entities in total)
• 機能のキーワード: amino acid transporter, aspartate transport, glutamate transporter homologue, transport protein, membrane protein
• 由来する生物種: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 137006.82

構造登録者

Arkhipova, V.,Slotboom, D.J.,Guskov, A. (登録日: 2020-01-24, 公開日: 2020-03-04, 最終更新日: 2025-07-02)

主引用文献

Arkhipova, V.,Guskov, A.,Slotboom, D.J.
Structural ensemble of a glutamate transporter homologue in lipid nanodisc environment.
Nat Commun, 11:998-998, 2020

PubMed Abstract: 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.

PubMed: 32081874
DOI: 10.1038/s41467-020-14834-8

実験手法

ELECTRON MICROSCOPY (3.38 Å)