Extended Data Fig. 6: Salicylate outcompetes SO42− in binding to anion-binding pocket.
From: The conformational cycle of prestin underlies outer-hair cell electromotility
a, The NLC measurements of HEK293T cells transfected with dolphin prestin in SO42− (0.15±0.06; n = 6). The NLC of these cells were completely abrogated (0.01±0.01) by 10 mM Na-Salicylate (mean ± s.e.m.; n, is the number of independent cells. One-sided student’s t-test, unpaired, P=0.01) b, Density of Salicylate (orange) in the anion-binding site (blue) was resolved in the Inhibited II (SO42−) state of dolphin prestin. c, Sequence alignment of prestin and close SLC transporters across different species. Residues forming the anion-binding site are largely conserved (e.g. Q97, F101, F137). Putative voltage-sensing residue R399 in dolphin prestin is replaced by a valine in murine SLC26A9. Clustal Omega was used for the sequence alignments. ChimeraX was used for illustration.
