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- PDB-9mun: Structure of Human SLC33A1 in complex with oxidized glutathione -

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Basic information

Entry
Database: PDB / ID: 9mun
TitleStructure of Human SLC33A1 in complex with oxidized glutathione
ComponentsAcetyl-coenzyme A transporter 1
KeywordsTRANSPORT PROTEIN / Glutathione
Function / homology
Function and homology information


acetyl-CoA transmembrane transporter activity / acetyl-CoA transmembrane transport / Transport of vitamins, nucleosides, and related molecules / Defective SLC33A1 causes spastic paraplegia 42 (SPG42) / transmembrane transport / Golgi membrane / endoplasmic reticulum membrane / protein homodimerization activity / membrane / plasma membrane
Similarity search - Function
Acetyl-coenzyme A transporter 1-like / Acetyl-coenzyme A transporter 1 / AmpG-like permease/Acetyl-coenzyme A transporter 1 / MFS transporter superfamily
Similarity search - Domain/homology
OXIDIZED GLUTATHIONE DISULFIDE / Acetyl-coenzyme A transporter 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.26 Å
AuthorsGad, M. / Hite, R.K.
Funding support1items
OrganizationGrant numberCountry
Other private
CitationJournal: Nat Cell Biol / Year: 2026
Title: SLC33A1 exports oxidized glutathione to maintain endoplasmic reticulum redox homeostasis.
Authors: Shanshan Liu / Mark Gad / Caifan Li / Kevin Cho / Yuyang Liu / Khando Wangdu / Viktor Belay / Alon Millet / Hiroyuki Kojima / Henry Sanford / Michele Wölk / Linas Urnavicius / Maria ...Authors: Shanshan Liu / Mark Gad / Caifan Li / Kevin Cho / Yuyang Liu / Khando Wangdu / Viktor Belay / Alon Millet / Hiroyuki Kojima / Henry Sanford / Michele Wölk / Linas Urnavicius / Maria Fedorova / Gary J Patti / Ekaterina V Vinogradova / Richard K Hite / Kıvanç Birsoy /
Abstract: The endoplasmic reticulum (ER) requires an oxidative environment to support the efficient maturation of secretory and membrane proteins. This is in part established by glutathione, a redox-active ...The endoplasmic reticulum (ER) requires an oxidative environment to support the efficient maturation of secretory and membrane proteins. This is in part established by glutathione, a redox-active metabolite present in reduced (GSH) and oxidized (GSSG) forms. The ER maintains a higher GSSG:GSH ratio than the cytosol; however, the mechanisms controlling ER redox balance remain poorly understood. To address this, we developed a method for the rapid immunopurification of the ER, enabling comprehensive profiling of its proteome and metabolome. Combining this approach with CRISPR screening, we identified SLC33A1 as the major ER GSSG exporter in mammalian cells. Loss of SLC33A1 led to GSSG accumulation in the ER and a liposome-based assay demonstrated that SLC33A1 directly transports GSSG. Cryogenic electron microscopy structures and molecular dynamics simulations revealed how SLC33A1 binds GSSG and identified residues critical for its transport. Finally, an imbalance in GSSG:GSH ratio induced ER stress and dependency on the ER-associated degradation pathway, driven by a shift in protein disulfide isomerases towards their oxidized forms. Together, our work establishes SLC33A1-mediated GSSG export as a key mechanism for ER redox homeostasis and protein maturation.
History
DepositionJan 14, 2025Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 25, 2026Provider: repository / Type: Initial release
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Acetyl-coenzyme A transporter 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)62,7732
Polymers62,1601
Non-polymers6131
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 Acetyl-coenzyme A transporter 1 / AT-1 / Acetyl-CoA transporter 1 / Solute carrier family 33 member 1


Mass: 62159.895 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SLC33A1, ACATN, AT1 / Production host: Homo sapiens (human) / References: UniProt: O00400
#2: Chemical ChemComp-GDS / OXIDIZED GLUTATHIONE DISULFIDE


Mass: 612.631 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C20H32N6O12S2 / 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: Human SLC33A1 with MAP tag insertion / Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: #1 / Source: RECOMBINANT
Molecular weightValue: 0.062 MDa / Experimental value: NO
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 7.4
Buffer component
IDConc.NameFormulaBuffer-ID
120 mMHepes1
2150 mMpotassium chlorideKCl1
30.01 percentLMNG1
40.001 percentCHS1
518 micromolarGDN1
SpecimenConc.: 5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 297 K

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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: DARK FIELD / Nominal defocus max: 1800 nm / Nominal defocus min: 800 nm
Image recordingElectron dose: 60 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k)

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Processing

EM software
IDNameVersionCategory
2PHENIX1.21.2_5419model refinement
12cryoSPARCclassification
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 3.26 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 215071 / Algorithm: FOURIER SPACE / Symmetry type: POINT
RefinementHighest resolution: 3.26 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0023826
ELECTRON MICROSCOPYf_angle_d0.4595221
ELECTRON MICROSCOPYf_dihedral_angle_d5.342515
ELECTRON MICROSCOPYf_chiral_restr0.035612
ELECTRON MICROSCOPYf_plane_restr0.004637

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