Supplementary Figure 4: Visualization of the domain interface and putative lipid density.
From: Cryo-EM structure of the human neutral amino acid transporter ASCT2
A single protomer of ASCT2 (a), EAAT1 (PDB 5LLU) (b), GltPh in the locked state (PDB 4X2S, chain A) (c) and GltPh in the unlocked state (PDB 4X2S, chain C) (d) viewed from the membrane plane. The scaffold domain is depicted as yellow ribbon and the transport domain in grey surface representation) with the interacting parts in black. The surface area of the interfaces are extensive in EAAT1 and locked GltPh. The transport domains in ACST2 and unlocked GltPh are more detached from the scaffold domain, but the shapes of their interaction surfaces are different, with most of the interacting residues in ASCT2 located in a narrow strip on the extracellular side. e, Patches of densities (green mesh at 4σ) observed between scaffold (yellow) and transport domain (blue) can accommodate cholesteryl hemisuccinate molecules shown as pink sticks, but the identities of the molecules could not be assigned unambiguously.
