Structural and functional characterization of protein-lipid interactions of the Salmonella typhimurium melibiose transporter MelB.

ABSTRACT:

Background

Membrane lipids play critical roles in the structure and function of membrane-embedded transporters. Salmonella typhimurium MelB (MelB_St) is a symporter coupling melibiose translocation with a cation (Na⁺, Li⁺, or H⁺). We present an extensive study on the effects of specific phospholipids on the structure of MelB_St and the melibiose transport catalyzed by this protein.

Results

Lipidomic analysis and thin-layer chromatography (TLC) experiments reveal that at least one phosphatidylethanolamine (PE) and one phosphatidylglycerol (PG) molecule associate with MelB_St at high affinities. Solid-state nuclear magnetic resonance (ssNMR) spectroscopy experiments confirmed the presence of lipid tails and glycero

SUBMITTER: Hariharan P 

PROVIDER: S-EPMC6091025 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature