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TitleStructure and mechanism of the human bile acid transporter OSTα-OSTβ.
Journal, issue, pagesNature, Vol. 651, Issue 8104, Page 251-259, Year 2026
Publish dateJan 28, 2026
AuthorsKe Wang / Junping Fan / Huiwen Chen / Bo Huang / Cheng Chi / Rui Yan / Di Wu / Feng Zhou / Wenhua Zhang / Juquan Jiang / Xiaoguang Lei / Daohua Jiang /
PubMed AbstractBile acids (BAs) are crucial amphipathic surfactants that function as multifaceted regulators in various physiological processes, including nutrient absorption and distribution, lipid metabolism and ...Bile acids (BAs) are crucial amphipathic surfactants that function as multifaceted regulators in various physiological processes, including nutrient absorption and distribution, lipid metabolism and inflammation. The human organic solute transporter αβ (OSTα-OSTβ; hereafter referred to as OSTα/β) is a BA transporter that has a key role in the secretion and distribution of BAs. Pathogenic mutations in OSTα/β have been associated with cholestasis. Despite the functional importance of OSTα/β in BA homeostasis, the stoichiometry and assembly of the complex and the molecular mechanism that underlies BA transport by OSTα/β remain unknown. Here we present cryo-electron microscopy structures of human OSTα/β in complex with cholesterols and an endogenous substrate, elucidating the structural basis for the function of OSTα/β. OSTα/β is assembled in a novel dimer-of-heterodimers manner: two OSTα units form the homodimeric core, with two OSTβ units bound to the periphery. OSTα adopts the G-protein-coupled-receptor (GPCR) fold and contains a unique cysteine-rich loop with seven palmitoylation sites; these cooperate with transmembrane helices 5 and 6, constituting a BA recognition site. A positive cavity in OSTα connects the BA site and facilitates the transmembrane translocation of BAs through OSTα/β. Together, this study reveals the architecture and transport mechanism of OSTα/β and provides insights into the structure-function relationships of this crucial transporter in BA homeostasis.
External linksNature / PubMed:41606314
MethodsEM (single particle)
Resolution2.64 - 2.73 Å
Structure data

63148

9ljg

EMDB-63148, PDB-9ljg:
Cryo-EM structure of human organic solute transporter OSTalpha/beta in apo state
Method: EM (single particle) / Resolution: 2.64 Å

63149

9ljh

EMDB-63149, PDB-9ljh:
Cryo-EM structure of human organic solute transporter OSTalpha/beta in complex with DHEAS
Method: EM (single particle) / Resolution: 2.73 Å

Chemicals

ChemComp-PLM:
PALMITIC ACID

ChemComp-LBN:
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine / phospholipid*YM

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-ZWY:
17-oxoandrost-5-en-3beta-yl hydrogen sulfate

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / transport / transport AD

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