Molecular architecture and the structural basis for anion interaction in prestin and SLC26 transporters.

ABSTRACT: Prestin (SLC26A5) is a member of the SLC26/SulP anion transporter family. Its unique quasi-piezoelectric mechanical activity generates fast cellular motility of cochlear outer hair cells, a key process underlying active amplification in the mammalian ear. Despite its established physiological role, it is essentially unknown how prestin can generate mechanical force, since structural information on SLC26/SulP proteins is lacking. Here we derive a structural model of prestin and related transporters by combining homology modelling, MD simulations and cysteine accessibility scanning. Prestin's transmembrane core region is organized in a 7+7 inverted repeat architecture. The model suggests a central cavity as the substrate-binding site located midway of the anion permeation pathway, which is s

SUBMITTER: Gorbunov D 

PROVIDER: S-EPMC3988826 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature