Extended Data Fig. 3: The conformational space of a GltPh protomer. | Nature

Extended Data Fig. 3: The conformational space of a GltPh protomer.

From: Glutamate transporters have a chloride channel with two hydrophobic gates

Extended Data Fig. 3

a, b, Front (a) and top (b) views of the cryo-EM map and atomic model of GltPh-XL2 in the iOFS (contour level 9.5σ) and ClCS (contour level 12.0σ). Density attributed to the scaffold domain, transport domain and HP2 are shown in salmon, blue and red, respectively. c, Conformational changes undertaken by a GltPh protomer during the substrate-transport cycle viewed from the side and top. HP2 is coloured for easier visualization of the rotational changes observed in the transport domain. d, e, Close-up views of the L152C–G351C crosslink fitted in the iOFS (d) (contour level 12.9σ) and ClCS (e) (contour level 10.3σ) cryo-EM maps. Contour levels were calculated using Chimera.

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