Extended Data Fig. 5: Nanodisc deformation supports transport-domain movement by the ClCS and putative lipid-binding sites.
From: Glutamate transporters have a chloride channel with two hydrophobic gates
a, Percentage of GltPh-XL2 trimers containing all three protomers in the iOFS, in the ClCS, or in a mixture of both states. Out of 220,938 trimers, 79,809 contained one or more protomers in the ClCS. Particle counting within symmetry-expanded data showed that 63,470 trimers contained one protomer in the ClCS, 14,394 trimers contained two protomers in the ClCS and 1,945 trimers contained all three protomers in the ClCS. b, Density map of GltPh-XL2 trimer (unfocused refinement) containing one ClCS protomer and embedded in nanodiscs (viewed from the membrane plane). The two iOFS protomers are shown in orange and the ClCS in blue. The nanodisc is shown in yellow. c, Putative lipid-binding sites in the GltPh-XL2 trimer, in which the transport domain is shown in blue and the scaffold domain in salmon. Identical lipid densities (green) were observed between protomers (contour level 7.2σ). Transmembrane helices located within 5 Å of the putative lipid densities are labelled. Contour levels were calculated using Chimera.
