Structural intermediates in a model of the substrate translocation path of the bacterial glutamate transporter homologue GltPh.

ABSTRACT: Excitatory amino acid transporters (EAATs) are membrane proteins responsible for reuptake of glutamate from the synaptic cleft to terminate neurotransmission and help prevent neurotoxically high, extracellular glutamate concentrations. Important structural information about these proteins emerged from crystal structures of GltPh, a bacterial homologue of EAATs, in conformations facing outward and inward. These remarkably different conformations are considered to be end points of the substrate translocation path (STP), suggesting that the transport mechanism involves major conformational rearrangements that remain uncharted. To investigate possible steps in the structural transitions of the STP between the two end-point conformations, we applied a combination of computational modeling metho

SUBMITTER: Stolzenberg S 

PROVIDER: S-EPMC3350225 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature