Fig. 6: Schematic representation of the GTR1 transport cycle.
From: Structural basis of glucosinolate recognition and transport by plant GTR1
a In the outward-facing conformation, the transporter exposes a large positively charged central cavity accessible to extracellular GLSs and protons. b Protonation of Glu75/Glu78 (in the E1X1X2E2K motif) enables GLS binding and leads to an occluded state. Subsequent protonation of Glu513 shifts the equilibrium toward the inward-facing conformation. c In the transition to the inward-facing state, protons dissociate from the protein, which facilitates GLS release from the transporter. d The unloaded transporter resets to the outward-facing state.
