Fig. 4: Mechanism of organic anion transport by Oat1.
From: Molecular basis for selective uptake and elimination of organic anions in the kidney by OAT1
a, Cryo-EM density of the phosphate molecule observed in site 1 (purple and threshold 0.341). Inset shows that the movement of Asp378 was observed between the α-KG bound state (wheat) and phosphate-bound state (blue). b, Mutational analysis of salt bridge interaction between TM8 and TM10. n = 15 independent experiments for the mutants and 80 for the wild-type errors shown are s.d. c, Cryo-EM density for the two rotamer positions of Tyr230 (purple and threshold 0.341). d, Analysis of the inward-facing structure (gray) with an outward open model (blue) reveals how key residues, as well as α-KG and the Cl− ion, align with where the helices pivot between states. Shown below are the salt bridge interactions identified from the outward open state that stabilize this conformation and form two ‘+−+’ motifs across the transporter. e, Oat1 contains three distinct ligand binding sites that could be targeted for selective inhibition.
