Fig. 2: The structure of taurine-bound TauT in the occluded state.
From: Dimerization and substrate recognition of human taurine transporter
A Overall structure of TauT. N terminus, C terminus, TM1-12, taurine and ions are labeled. TM1, TM6, N terminus and C terminus are in blue colors. B, C Recognition of taurine by TauT. The densities for taurine, Na1, Na2 and Cl- are represented in mesh. The surrounding interaction residues are shown in sticks. D–F Coordinations of Na1 (D), Na2 (E) and Cl- (F) ions. Potential hydrogen bonds are represented in red dash lines. G, H Detailed views of the extensive interactions in the N terminus (G) and C terminus (H). Cryo-EM densities for N terminus and C terminus are shown in partially transparent surface. The critical residues are indicated and labeled. I The relative uptake activities of the WT TauT and the indicated mutants to explore the importance of the residues involved in coordinating with taurine and ions. Each point is mean ± SD. from three independent experiments, each with a single measurement (n = 3).
