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- PDB-9ljg: Cryo-EM structure of human organic solute transporter OSTalpha/be... -

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Basic information

Entry
Database: PDB / ID: 9ljg
TitleCryo-EM structure of human organic solute transporter OSTalpha/beta in apo state
Components
  • Organic solute transporter subunit alpha
  • Organic solute transporter subunit beta
KeywordsTRANSPORT PROTEIN / transport
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
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine / PALMITIC ACID / CHOLESTEROL HEMISUCCINATE / 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: 2.64 Å
AuthorsWang, K. / Jiang, D.H.
Funding support China, 1items
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, 2025Deposition site: PDBJ / Processing site: PDBC
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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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)115,75832
Polymers104,2604
Non-polymers11,49828
Water00
1


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

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Components

#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
#3: Chemical
ChemComp-PLM / PALMITIC ACID


Mass: 256.424 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: C16H32O2 / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical
ChemComp-LBN / 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine / (2R)-2-[(9Z)-9-Octadecenoyloxy]-3-(palmitoyloxy)propyl 2-(trimethylammonio)ethyl phosphate


Mass: 760.076 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C42H82NO8P / Feature type: SUBJECT OF INVESTIGATION / Comment: phospholipid*YM
#5: Chemical
ChemComp-Y01 / CHOLESTEROL HEMISUCCINATE


Mass: 486.726 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C31H50O4 / Feature type: SUBJECT OF INVESTIGATION
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: Transport AC / Type: COMPLEX / Entity ID: #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

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM software
IDNameVersionCategory
1cryoSPARC4.6.0particle selection
13cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 2.64 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 93268 / Symmetry type: POINT

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