8TNY

Substrate Binding Plasticity Revealed by Cryo-EM Structures of SLC26A2

8TNY の概要

• エントリーDOI: 10.2210/pdb8tny/pdb
• EMDBエントリー: 41427 41428 41429
• 分子名称: Sulfate transporter, SULFATE ION (2 entities in total)
• 機能のキーワード: human solute carrier, slc26a2, sulfate transporter, membrane protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 149012.84

構造登録者

Hu, W.,Song, A. (登録日: 2023-08-02, 公開日: 2024-05-22)

主引用文献

Hu, W.,Song, A.,Zheng, H.
Substrate binding plasticity revealed by Cryo-EM structures of SLC26A2.
Nat Commun, 15:3616-3616, 2024

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: 38684689
DOI: 10.1038/s41467-024-48028-3

実験手法

ELECTRON MICROSCOPY (3.55 Å)