Time-resolved mechanism of extracellular gate opening and substrate binding in a glutamate transporter.

ABSTRACT: Glutamate transporters, also referred to as excitatory amino acid transporters (EAATs), are membrane proteins that regulate glutamatergic signal transmission by clearing excess glutamate after its release at synapses. A structure-based understanding of their molecular mechanisms of function has been elusive until the recent determination of the x-ray structure of an archaeal transporter, Glt(Ph). Glt(Ph) exists as a trimer, with each subunit containing a core region that mediates substrate translocation. In the present study a series of molecular dynamics simulations have been conducted and analyzed in light of new experimental data on substrate binding properties of EAATs. The simulations provide for the first time a full atomic description of the time-resolved events that drive the recog

SUBMITTER: Shrivastava IH 

PROVIDER: S-EPMC2568915 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature