Distinct roles of the major binding residues in the cation-binding pocket of the melibiose transporter MelB.

ABSTRACT: Salmonella enterica serovar Typhimurium melibiose permease (MelB_St) is a prototype of the major facilitator superfamily (MFS) transporters, which play important roles in human health and diseases. MelB_St catalyzed the symport of galactosides with Na⁺, Li⁺, or H⁺ but prefers the coupling with Na⁺. Previously, we determined the structures of the inward- and outward-facing conformation of MelB_St and the molecular recognition for galactoside and Na⁺. However, the molecular mechanisms for H⁺- and Na⁺-coupled symport remain poorly understood. In this study, we solved two x-ray crystal structures of MelB_St, the cation-binding site mutants D59C at an unliganded apo-state and D55

SUBMITTER: Hariharan P 

PROVIDER: S-EPMC11259710 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature