Structural ensemble of a glutamate transporter homologue in lipid nanodisc environment
Valentina Arkhipova,
Albert Guskov () and
Dirk J. Slotboom ()
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Valentina Arkhipova: University of Groningen
Albert Guskov: University of Groningen
Dirk J. Slotboom: University of Groningen
Nature Communications, 2020, vol. 11, issue 1, 1-9
Abstract:
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 GltTk, 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.
Date: 2020
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14834-8
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DOI: 10.1038/s41467-020-14834-8
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