8GK6

Crystal structure of extracellular domain of CNNM4 from Echinococcus granulosus

8GK6 の概要

• エントリーDOI: 10.2210/pdb8gk6/pdb
• 分子名称: Metal transporter CNNM4, alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• 機能のキーワード: immunoglobulin-like fold, beta-sandwich, magnesium transporter, metal transport
• 由来する生物種: Echinococcus granulosus
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 128735.30

構造登録者

Shahsavan, A.,Gehring, K. (登録日: 2023-03-17, 公開日: 2023-12-13, 最終更新日: 2024-02-07)

主引用文献

Shahsavan, A.,Lee, E.L.,Illes, K.,Kozlov, G.,Gehring, K.
Dimerization of the CNNM extracellular domain.
Protein Sci., 33:e4860-e4860, 2024

PubMed Abstract: Cystathionine- -synthase (CBS)-pair domain divalent metal cation transport mediators (CNNMs) are an evolutionarily conserved family of magnesium transporters. They mediate magnesium homeostasis directly by transport of Mg ions and indirectly by regulation of the transient receptor potential ion channel subfamily M member 7 (TRPM7). Here, we report the crystal structure of the extracellular domain of tapeworm CNNM4. The domain forms a dimer of immunoglobulin-like (Ig-like) folds with electron density observed for three glycosylation sites. Analytical ultracentrifugation confirms that mutations in the extracellular domain of human CNNM4 prevent its dimerization. An analogous mutation in mouse CNNM2 impairs its activity in a cellular assay of Mg transport.

PubMed: 38149326
DOI: 10.1002/pro.4860

実験手法

X-RAY DIFFRACTION (2.7 Å)