Fig. 4: Conformational plasticity of ASCT2 protomers in lipid nanodiscs identified under substrate-bound and substrate-free conditions.
From: Structural basis of the obligatory exchange mode of human neutral amino acid transporter ASCT2

a Structures of substrate-bound ASCT2 at three distinct conformational states: Gln-Na+-OFSHP2cld (blue), Gln-Na+-iOFS-upHP2cld (light pink), and Gln-Na+-iOFS-downHP2cld (teal). b Structures of substrate-free ASCT2 at two distinct conformational states: Na+-depleted OFSHP2op (blue) and Na+-depleted iOFS-upHP2op (light pink). Each protomer is shown as a cartoon representation of the transport domain displayed in unique colors, and a surface colored in gray represents the scaffold domain. The scaffold domain acts as a reference point for the position of the transport domain in the membrane. The HP2 is displayed in salmon (closed conformation as seen in a) or purple (open conformation as seen in b).