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- PDB-9wpz: cryo-EM structure of human organic solute transporter in complex ... -

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Basic information

Entry
Database: PDB / ID: 9wpz
Titlecryo-EM structure of human organic solute transporter in complex with TLCA
Components(Organic solute transporter subunit ...) x 2
KeywordsTRANSPORT PROTEIN / TLCA / TRANSPORTER
Function / homology
Function and homology information


bile acid secretion / bile acid transmembrane transporter activity / Recycling of bile acids and salts / bile acid and bile salt transport / transmembrane transporter activity / basolateral plasma membrane / protein heterodimerization activity / endoplasmic reticulum membrane / protein homodimerization activity / protein-containing complex ...bile acid secretion / bile acid transmembrane transporter activity / Recycling of bile acids and salts / bile acid and bile salt transport / transmembrane transporter activity / 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
: / CHOLESTEROL / PALMITIC ACID / Chem-POV / Organic solute transporter subunit alpha / Organic solute transporter subunit beta
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.11 Å
AuthorsSun, X. / Yao, D. / Xue, J.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)NCTIB2022HS02004 China
CitationJournal: Nat Struct Mol Biol / Year: 2026
Title: Structural insights into OSTα/β-mediated transport of bile acids and steroid conjugates.
Authors: Xicheng Sun / Taikun Tian / Minying Low / Shaobai Li / Deqiang Yao / Yanmei Yuan / Mi Cao / Ming Lei / Yong Wang / Hongwen Chen / Pengfei Lan / Qiang Xia / Jing Xue /
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 ...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.
History
DepositionSep 10, 2025Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Jun 10, 2026Provider: repository / Type: Initial release
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Organic solute transporter subunit alpha
B: Organic solute transporter subunit beta
C: Organic solute transporter subunit alpha
D: Organic solute transporter subunit beta
hetero molecules


Theoretical massNumber of molelcules
Total (without water)117,24536
Polymers104,2604
Non-polymers12,98432
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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Organic solute transporter subunit ... , 2 types, 4 molecules ACBD

#1: Protein Organic solute transporter subunit alpha / OST-alpha / Solute carrier family 51 subunit alpha


Mass: 37768.938 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SLC51A, OSTA / Production host: Homo sapiens (human) / References: UniProt: Q86UW1
#2: Protein Organic solute transporter subunit beta / OST-beta / Solute carrier family 51 subunit beta


Mass: 14361.263 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SLC51B, OSTB / Production host: Homo sapiens (human) / References: UniProt: Q86UW2

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Non-polymers , 4 types, 32 molecules

#3: Chemical
ChemComp-CLR / CHOLESTEROL


Mass: 386.654 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C27H46O
#4: Chemical
ChemComp-PLM / PALMITIC ACID


Mass: 256.424 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: C16H32O2
#5: Chemical
ChemComp-POV / (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / POPC


Mass: 760.076 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C42H82NO8P / Comment: phospholipid*YM
#6: Chemical ChemComp-A1EPX / Taurolithocholic Acid


Mass: 483.704 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C26H45NO5S / Feature type: SUBJECT OF INVESTIGATION

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Details

Has ligand of interestY
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: cryo-EM structure of human organic solute transporter in complex with TLCA
Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 7.5
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

MicroscopyModel: FEI/PHILIPS CM300FEG/T
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 1700 nm / Nominal defocus min: 900 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM software
IDNameVersionCategory
1Gautomatchparticle selection
2PHENIX1.20.1_4487model refinement
13cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.11 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 453346 / Symmetry type: POINT
RefinementHighest resolution: 3.11 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0036903
ELECTRON MICROSCOPYf_angle_d0.5889290
ELECTRON MICROSCOPYf_dihedral_angle_d10.7591911
ELECTRON MICROSCOPYf_chiral_restr0.0381095
ELECTRON MICROSCOPYf_plane_restr0.0061026

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