Fig. 1: Structural and biochemical characterization of b0,+AT–rBAT in a lipid environment. | Nature Communications

Fig. 1: Structural and biochemical characterization of b0,+AT–rBAT in a lipid environment.

From: Ca2+-mediated higher-order assembly of heterodimers in amino acid transport system b0,+ biogenesis and cystinuria

Fig. 1: Structural and biochemical characterization of b0,+AT–rBAT in a lipid environment.

a 2D class averages of ovine and murine b0,+AT–rBAT imaged by negative-stain electron microscopy. The rBAT ectodomains are marked by yellow arrows. b 2D class averages of LAT1–CD98hc. The CD98hc ectodomain is marked by a yellow arrow. c Uptake of ʟ-[3H]Arg by ovine b0,+AT–rBAT reconstituted into proteoliposomes. Proteoliposomes were pre-loaded with either 1 mM or no ʟ-Arg. Control experiments were performed with protein-free liposomes. Values are mean ± SEM. n = 3 technical replicates. d Cryo-EM map of the super-dimeric b0,+AT–rBAT complex in lipid nanodiscs. Map densities corresponding to different chains and chemical identities are colored as follows: rBAT (green and light green), b0,+AT (cyan and light cyan), nanodisc (translucent white), lipids (yellow) and N-linked glycans (orange). e Ribbon diagram of b0,+AT–rBAT. The position of the lipid bilayer is based on the lipid-solvent boundaries calculated by the PPM server (https://opm.phar.umich.edu/ppm_server).

Back to article page