Large-scale state-dependent membrane remodeling by a transporter protein.

ABSTRACT: That channels and transporters can influence the membrane morphology is increasingly recognized. Less appreciated is that the extent and free-energy cost of these deformations likely varies among different functional states of a protein, and thus, that they might contribute significantly to defining its mechanism. We consider the trimeric Na⁺-aspartate symporter Glt_Ph, a homolog of an important class of neurotransmitter transporters, whose mechanism entails one of the most drastic structural changes known. Molecular simulations indicate that when the protomers become inward-facing, they cause deep, long-ranged, and yet mutually-independent membrane deformations. Using a novel simulation methodology, we estimate that the free-energy cost of this membrane perturbation i

SUBMITTER: Zhou W 

PROVIDER: S-EPMC6957315 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature