Molecular Basis for the Cation Selectivity of Salmonella typhimurium Melibiose Permease.

ABSTRACT: Cation selectivity and coupling are important attributes of cation-coupled symporters. Salmonella typhimurium melibiose permease (MelB_St) catalyzes the co-transport of galactosides with cations (H⁺, Li⁺, or Na⁺). 3-D crystal structures of MelB_St have revealed the molecular recognition for sugar substrates, but the cation binding and coupling mechanisms have not been defined to atomic levels. In its human homolog MFSD2A, a lethal mutation was mapped at its Na⁺-binding pocket; however, none of the structures in this subfamily resolved its cation binding. In this study, molecular dynamics simulations reveal the binding interactions of Na⁺ and Li⁺ with MelB_St. Interestingly, Thr121, the lethal mu

SUBMITTER: Katsube S 

PROVIDER: S-EPMC9177823 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature