Constraints imposed by the membrane selectively guide the alternating access dynamics of the glutamate transporter GltPh.

ABSTRACT: Substrate transport in sodium-coupled amino acid symporters involves a large-scale conformational change that shifts the access to the substrate-binding site from one side of the membrane to the other. The structural change is particularly substantial and entails a unique piston-like quaternary rearrangement in glutamate transporters, as evidenced by the difference between the outward-facing and inward-facing structures resolved for the archaeal aspartate transporter Glt(Ph). These structural changes occur over time and length scales that extend beyond the reach of current fully atomic models, but are regularly explored with the use of elastic network models (ENMs). Despite their success with other membrane proteins, ENM-based approaches for exploring the collective dynamics of Glt(Ph) hav

SUBMITTER: Lezon TR 

PROVIDER: S-EPMC3309413 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature