ArticleNature structural & molecular biology2026
Structural insights into OSTα/β-mediated transport of bile acids and steroid conjugates.
Article in Nature structural & molecular biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Mammalian organic solute transporter α/β (OSTα/β) is crucial for the enterohepatic circulation of bile acids and the homeostasis of steroid conjugates, mediating their movement across membranes as an obligate heterodimer. Here we present high-resolution cryo-EM structures of human OSTα/β in apo, substrate-bound and inhibitor-bound states, revealing a tetrameric organization as a homodimer of heterodimers that is required for membrane activity. Substrates bind within a surface-exposed tunnel formed by transmembrane helices 5 and 6, which is unexpectedly sealed by multiple palmitoyl chains covalently attached to a conserved intracellular loop IL2. Two chemically distinct inhibitors, fidaxomicin and ethinylestradiol, disrupt transport by both competing for the substrate-binding pocket and sterically occluding the tunnel. Together with biochemical and evolutionary analyses, our work defines a distinctive class of solute carriers that uses palmitoylation to facilitate substrate transport, a mechanism conserved across eukaryotes.
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