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- EMDB-63148: Cryo-EM structure of human organic solute transporter OSTalpha/be... -

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Basic information

Entry
Database: EMDB / ID: EMD-63148
TitleCryo-EM structure of human organic solute transporter OSTalpha/beta in apo state
Map data
Sample
  • Complex: Transport AC
    • Protein or peptide: Organic solute transporter subunit beta
  • Protein or peptide: Organic solute transporter subunit alpha
  • Ligand: PALMITIC ACID
  • Ligand: 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine
  • Ligand: CHOLESTEROL HEMISUCCINATE
Keywordstransport / TRANSPORT PROTEIN
Function / homology
Function and homology information


bile acid secretion / positive regulation of glycoprotein biosynthetic process / positive regulation of protein exit from endoplasmic reticulum / bile acid transmembrane transporter activity / bile acid and bile salt transport / transmembrane transporter activity / positive regulation of protein targeting to membrane / Recycling of bile acids and salts / regulation of protein stability / basolateral plasma membrane ...bile acid secretion / positive regulation of glycoprotein biosynthetic process / positive regulation of protein exit from endoplasmic reticulum / bile acid transmembrane transporter activity / bile acid and bile salt transport / transmembrane transporter activity / positive regulation of protein targeting to membrane / Recycling of bile acids and salts / regulation of protein stability / basolateral plasma membrane / protein heterodimerization activity / endoplasmic reticulum membrane / protein homodimerization activity / protein-containing complex / membrane / plasma membrane
Similarity search - Function
Organic solute transporter subunit beta / : / Organic solute transporter subunit beta protein / Organic solute transporter subunit alpha/Transmembrane protein 184 / Organic solute transporter Ostalpha / Organic solute transporter Ostalpha
Similarity search - Domain/homology
Organic solute transporter subunit alpha / Organic solute transporter subunit beta
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.64 Å
AuthorsWang K / Jiang DH
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)31971134 China
CitationJournal: Nature / Year: 2026
Title: Structure and mechanism of the human bile acid transporter OSTα-OSTβ.
Authors: Ke Wang / Junping Fan / Huiwen Chen / Bo Huang / Cheng Chi / Rui Yan / Di Wu / Feng Zhou / Wenhua Zhang / Juquan Jiang / Xiaoguang Lei / Daohua Jiang /
Abstract: Bile 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.
History
DepositionJan 15, 2025-
Header (metadata) releaseDec 3, 2025-
Map releaseDec 3, 2025-
UpdateMar 18, 2026-
Current statusMar 18, 2026Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_63148.png

Downloads & links

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Map

FileDownload / File: emd_63148.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.85 Å/pix.
x 320 pix.
= 272. Å		0.85 Å/pix.
x 320 pix.
= 272. Å		0.85 Å/pix.
x 320 pix.
= 272. Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.85 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.87
Minimum - Maximum-2.8758817 - 4.9184847
Average (Standard dev.)-0.0009083088 (±0.121816345)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 272.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_63148_half_map_1.map
Projections & Slices
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Histogram (log scale)

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Half map: #1

Fileemd_63148_half_map_2.map
Projections & Slices
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Histogram (log scale)

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Sample components

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Entire : Transport AC

EntireName: Transport AC
Components
  • Complex: Transport AC
    • Protein or peptide: Organic solute transporter subunit beta
  • Protein or peptide: Organic solute transporter subunit alpha
  • Ligand: PALMITIC ACID
  • Ligand: 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine
  • Ligand: CHOLESTEROL HEMISUCCINATE

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Supramolecule #1: Transport AC

SupramoleculeName: Transport AC / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #2
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Organic solute transporter subunit alpha

MacromoleculeName: Organic solute transporter subunit alpha / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 37.768938 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MEPGRTQIKL DPRYTADLLE VLKTNYGIPS ACFSQPPTAA QLLRALGPVE LALTSILTLL ALGSIAIFLE DAVYLYKNTL CPIKRRTLL WKSSAPTVVS VLCCFGLWIP RSLVLVEMTI TSFYAVCFYL LMLVMVEGFG GKEAVLRTLR DTPMMVHTGP C CCCCPCCP ...String:
MEPGRTQIKL DPRYTADLLE VLKTNYGIPS ACFSQPPTAA QLLRALGPVE LALTSILTLL ALGSIAIFLE DAVYLYKNTL CPIKRRTLL WKSSAPTVVS VLCCFGLWIP RSLVLVEMTI TSFYAVCFYL LMLVMVEGFG GKEAVLRTLR DTPMMVHTGP C CCCCPCCP RLLLTRKKLQ LLMLGPFQYA FLKITLTLVG LFLVPDGIYD PADISEGSTA LWINTFLGVS TLLALWTLGI IS RQARLHL GEQNMGAKFA LFQVLLILTA LQPSIFSVLA NGGQIACSPP YSSKTRSQVM NCHLLILETF LMTVLTRMYY RRK DHKVGY ETFSSPDLDL NLKA

UniProtKB: Organic solute transporter subunit alpha

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Macromolecule #2: Organic solute transporter subunit beta

MacromoleculeName: Organic solute transporter subunit beta / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 14.361263 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MEHSEGAPGD PAGTVVPQEL LEEMLWFFRV EDASPWNHSI LALAAVVVII SMVLLGRSIQ ASRKEKMQPP EKETPEVLHL DEAKDHNSL NNLRETLLSE KPNLAQVELE LKERDVLSVF LPDVPETES

UniProtKB: Organic solute transporter subunit beta

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Macromolecule #3: PALMITIC ACID

MacromoleculeName: PALMITIC ACID / type: ligand / ID: 3 / Number of copies: 14 / Formula: PLM
Molecular weightTheoretical: 256.424 Da
Chemical component information

ChemComp-PLM:
PALMITIC ACID

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Macromolecule #4: 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine

MacromoleculeName: 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine / type: ligand / ID: 4 / Number of copies: 4 / Formula: LBN
Molecular weightTheoretical: 760.076 Da
Chemical component information

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

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Macromolecule #5: CHOLESTEROL HEMISUCCINATE

MacromoleculeName: CHOLESTEROL HEMISUCCINATE / type: ligand / ID: 5 / Number of copies: 10 / Formula: Y01
Molecular weightTheoretical: 486.726 Da
Chemical component information

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.64 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 93268
Initial angle assignmentType: RANDOM ASSIGNMENT
Final angle assignmentType: MAXIMUM LIKELIHOOD

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