8TNX
Substrate Binding Plasticity Revealed by Cryo-EM Structures of SLC26A2
Summary for 8TNX
| Entry DOI | 10.2210/pdb8tnx/pdb |
| EMDB information | 41427 41428 41429 |
| Descriptor | Sulfate transporter, OXALATE ION (2 entities in total) |
| Functional Keywords | slc26a2, sulfate transporter, membrane protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 148996.76 |
| Authors | |
| Primary citation | Hu, W.,Song, A.,Zheng, H. Substrate binding plasticity revealed by Cryo-EM structures of SLC26A2. Nat Commun, 15:3616-3616, 2024 Cited by PubMed 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 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. PubMed: 38684689DOI: 10.1038/s41467-024-48028-3 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.03 Å) |
Structure validation
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