Conformational free energy landscape of a glutamate transporter and microscopic details of its transport mechanism.

ABSTRACT: Removing glutamate from the synaptic cleft is vital for proper function of the brain. Excitatory amino acid transporters mediate this process by uptaking the neurotransmitter from the synaptic cleft back to the cell after its release. The archaeal homolog, Glt_Ph, an aspartate transporter from Pyrococcus horikoshii, presents the best structurally characterized model for this family of transporters. In order to transport, Glt_Ph undergoes elevator-like conformational changes between inward-facing (IF) and outward-facing (OF) states. Here, we characterize, at an atomic level, the OF⇌IF transition of Glt_Ph in different apo/bound states using a combination of ensemble-based enhanced sampling techniques, employing more than two thousand of coupled si

SUBMITTER: Thangapandian S 

PROVIDER: S-EPMC11912404 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature