Fig. 4: Comparison between the SLC26A9 structure and similar structures.
From: Structural insights into the gating mechanism of human SLC26A9 mediated by its C-terminal sequence
a A superposition of the structures of human SLC26A9 and mouse Slc26a9. The major difference lies in the α extension of the STAS domain and the C-terminal sequence. b Enlarged view of the α extension. c Enlarged view of the C-terminal sequence. d Human SLC26A9 and SLC26Dg (PDB ID: 5IOF) aligned by the ion permeation pathway. SLC26Dg is colored cyan, and SLC26A9 is colored brown. The substituted residues are colored according to their relative charge, with blue representing more electropositivity and red representing more electronegativity. e Human SLC26A9 and human SLC4A1 (PDB ID: 4YZF) aligned by their gate domains. As SLC4A1 is solved in the outward-facing conformation, conformation differences in the core domains further support the elevator alternative-access model of SLC26A9. TM3 and TM10 are enlarged to depict the movement.
