Structural ensemble of a glutamate transporter homologue in lipid nanodisc environment.

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_Tk, 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

SUBMITTER: Arkhipova V 

PROVIDER: S-EPMC7035293 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature