Fig. 1: Cryo-EM structure of BTR1 in the outward-facing state.
From: Structural insights into the conformational changes of BTR1/SLC4A11 in complex with PIP2
a I–V curve of cells expressing wild-type BTR1 at pH 7.4 in the presence and absence of 5 mM NH4Cl. The current values are standardized by cell capacitance. Data shown are mean values ± s.d. of n = 4 biologically independent experiments. b Topology and domain arrangement of a BTR1 monomer. The gate domain, core domain and N-terminal cytoplasmic domain (NTD) are shown in blue, green and pink, respectively. Gray bars represent the boundaries of the cell membrane. c, d Cryo-EM maps of the outward-facing state of a BTR1 dimer bound to PIP2: views from the side (c) and the bottom (d). The two monomers of BTR1 are colored in blue and green, and the PIP2 molecules are colored in gold. The remaining lipid molecules are shown as transparent gray. e, f Structural model of the outward-facing state BTR1 views from the side (e) and the bottom (f). The two PIP2 molecules are shown in stick representations. The color scheme of one BTR1 monomer is the same as in (b), and the other monomer is colored in gray.
