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- PDB-8tny: Substrate Binding Plasticity Revealed by Cryo-EM Structures of SLC26A2 -

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Basic information

Entry
Database: PDB / ID: 8tny
TitleSubstrate Binding Plasticity Revealed by Cryo-EM Structures of SLC26A2
ComponentsSulfate transporter
KeywordsMEMBRANE PROTEIN / human solute carrier / SLC26A2 / sulfate transporter
Function / homology
Function and homology information


Defective SLC26A2 causes chondrodysplasias / sulfate transmembrane transport / Multifunctional anion exchangers / Transport and synthesis of PAPS / sulfate transport / sulfate transmembrane transporter activity / chondrocyte proliferation / secondary active sulfate transmembrane transporter activity / oxalate transmembrane transporter activity / solute:inorganic anion antiporter activity ...Defective SLC26A2 causes chondrodysplasias / sulfate transmembrane transport / Multifunctional anion exchangers / Transport and synthesis of PAPS / sulfate transport / sulfate transmembrane transporter activity / chondrocyte proliferation / secondary active sulfate transmembrane transporter activity / oxalate transmembrane transporter activity / solute:inorganic anion antiporter activity / bicarbonate transmembrane transporter activity / chloride transmembrane transporter activity / microvillus membrane / chondrocyte differentiation / ossification / apical plasma membrane / extracellular exosome / membrane / plasma membrane
Similarity search - Function
Sulphate anion transporter, conserved site / SLC26A transporters signature. / SLC26A/SulP transporter / SLC26A/SulP transporter domain / Sulfate permease family / STAS domain / STAS domain profile. / STAS domain / STAS domain superfamily
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.55 Å
AuthorsHu, W. / Song, A.
Funding support United States, 3items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM126626 United States
National Institutes of Health/National Institute on Aging (NIH/NIA)AG064572 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI175646 United States
CitationJournal: Nat Commun / Year: 2024
Title: Substrate binding plasticity revealed by Cryo-EM structures of SLC26A2.
Authors: Wenxin Hu / Alex Song / Hongjin Zheng
Abstract: SLC26A2 is a vital solute carrier responsible for transporting essential nutritional ions, including sulfate, within the human body. Pathogenic mutations within SLC26A2 give rise to a spectrum of ...SLC26A2 is a vital solute carrier responsible for transporting essential nutritional ions, including sulfate, within the human body. Pathogenic mutations within SLC26A2 give rise to a spectrum of human diseases, ranging from lethal to mild symptoms. The molecular details regarding the versatile substrate-transporter interactions and the impact of pathogenic mutations on SLC26A2 transporter function remain unclear. Here, using cryo-electron microscopy, we determine three high-resolution structures of SLC26A2 in complexes with different substrates. These structures unveil valuable insights, including the distinct features of the homodimer assembly, the dynamic nature of substrate binding, and the potential ramifications of pathogenic mutations. This structural-functional information regarding SLC26A2 will advance our understanding of cellular sulfate transport mechanisms and provide foundations for future therapeutic development against various human diseases.
History
DepositionAug 2, 2023Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 22, 2024Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
B: Sulfate transporter
A: Sulfate transporter
hetero molecules


Theoretical massNumber of molelcules
Total (without water)149,0134
Polymers148,8212
Non-polymers1922
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein Sulfate transporter / Diastrophic dysplasia protein / Solute carrier family 26 member 2


Mass: 74410.359 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SLC26A2, DTD, DTDST / Production host: Escherichia coli (E. coli) / References: UniProt: P50443
#2: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4 / Feature type: SUBJECT OF INVESTIGATION
Has ligand of interestY

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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: SLC26A2 with sulfate / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 7.4
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: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2500 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 60 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

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Processing

CTF correctionType: NONE
3D reconstructionResolution: 3.55 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 141916 / Symmetry type: POINT

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