Going Outside the TonB Box: Identification of Novel FepA-TonB Interactions In Vivo.

ABSTRACT: In Gram-negative bacteria, the cytoplasmic membrane protein TonB transmits energy derived from proton motive force to energize transport of important nutrients through TonB-dependent transporters in the outer membrane. Each transporter consists of a beta barrel domain and a lumen-occluding cork domain containing an essential sequence called the TonB box. To date, the only identified site of transporter-TonB interaction is between the TonB box and residues ∼158 to 162 of TonB. While the mechanism of ligand transport is a mystery, a current model based on site-directed spin labeling and molecular dynamics simulations is that, following ligand binding, the otherwise-sequestered TonB box extends into the periplasm for recognition by TonB, which mediates transport by pulling or twisting the cor

SUBMITTER: Gresock MG 

PROVIDER: S-EPMC5405211 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature