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- PDB-8tnx: Substrate Binding Plasticity Revealed by Cryo-EM Structures of SLC26A2 -
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Open data
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Basic information
Entry | Database: PDB / ID: 8tnx | ||||||||||||
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Title | Substrate Binding Plasticity Revealed by Cryo-EM Structures of SLC26A2 | ||||||||||||
![]() | Sulfate transporter | ||||||||||||
![]() | MEMBRANE PROTEIN / SLC26A2 / sulfate transporter | ||||||||||||
Function / homology | ![]() 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 | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.03 Å | ||||||||||||
![]() | Hu, W. / Song, A. | ||||||||||||
Funding support | ![]()
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![]() | ![]() 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 |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 219.4 KB | Display | ![]() |
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PDB format | ![]() | 169.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 41428MC ![]() 8tnwC ![]() 8tnyC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 74410.359 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: SLC26A2 with oxalate / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT |
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Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() ![]() |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1000 nm |
Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
CTF correction | Type: NONE |
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3D reconstruction | Resolution: 3.03 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 137202 / Symmetry type: POINT |