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Structure paper

TitleStructures of Ostα/β reveal a unique fold and bile acid transport mechanism.
Journal, issue, pagesNature, Year 2026
Publish dateJan 28, 2026
AuthorsXuemei Yang / Nana Cui / Tianyu Li / Xinheng He / Heng Zhang / Canrong Wu / Yang Li / Xiong Ma / H Eric Xu /
PubMed AbstractBile acid and steroid hormone homeostasis are critical for human health, with disruptions linked to metabolic and endocrine disorders. The organic solute transporter Ostα/β, essential for bile acid ...Bile acid and steroid hormone homeostasis are critical for human health, with disruptions linked to metabolic and endocrine disorders. The organic solute transporter Ostα/β, essential for bile acid efflux in enterohepatic circulation, has long defied mechanistic elucidation. Here we present cryogenic electron microscopy structures of human Ostα/β in apo and substrate-bound states at 2.6-3.1 Å resolution, revealing a distinctive membrane protein architecture that defines a new transporter class. Ostα/β forms a symmetric tetramer of heterodimers, with each Ostα subunit showing a new seven-transmembrane fold, augmented by a single transmembrane helix of Ostβ. This architecture is stabilized by extensive lipid modifications, including a palmitoylated cysteine-rich motif that forms a lateral substrate-binding groove. The structures uncover a unique transport pathway featuring two substrate-binding sites connected by an amphipathic helix-gated conduit. This design, conserved in the evolutionarily related TMEM184 family, suggests an ancient mechanism for substrate translocation. Electrophysiological studies demonstrate voltage-sensitive, bidirectional transport driven by electrochemical gradients, elucidating the efflux role of Ostα/β in vivo. Lipid interactions, notably palmitoylation-dependent trafficking, emerge as critical for stability and function. These findings clarify the molecular mechanism of Ostα/β, provide a structural basis for disease-associated mutations and establish a paradigm for lipid-modified membrane transport.
External linksNature / PubMed:41606328
MethodsEM (single particle)
Resolution2.6 - 3.12 Å
Structure data

64364

9unv

EMDB-64364, PDB-9unv:
Cryo-EM structure of human organic solute transporter Ost-alpha/beta bound with TLCA
Method: EM (single particle) / Resolution: 3.12 Å

64369

9uo1

EMDB-64369, PDB-9uo1:
Cryo-EM structure of human organic solute transporter Ost-alpha/beta bound with DHEAS
Method: EM (single particle) / Resolution: 2.9 Å

64370

9uo2

EMDB-64370, PDB-9uo2:
Cryo-EM structure of human organic solute transporter Ost-alpha/beta in apo state
Method: EM (single particle) / Resolution: 2.6 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL

ChemComp-P0E:
PHOSPHATIDYL ETHANOL

ChemComp-LPE:
1-O-OCTADECYL-SN-GLYCERO-3-PHOSPHOCHOLINE

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-PLM:
PALMITIC ACID

PDB-1epx:
CRYSTAL STRUCTURE ANALYSIS OF ALDOLASE FROM L. MEXICANA

ChemComp-76F:
(7E,21R,24S)-27-amino-24-hydroxy-18,24-dioxo-19,23,25-trioxa-24lambda~5~-phosphaheptacos-7-en-21-yl (9Z,12E)-octadeca-9,12-dienoate

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

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / Complex / bile acids / substrate / transport / heterodimer

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