8GK6
Crystal structure of extracellular domain of CNNM4 from Echinococcus granulosus
Summary for 8GK6
| Entry DOI | 10.2210/pdb8gk6/pdb |
| Descriptor | 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) |
| Functional Keywords | immunoglobulin-like fold, beta-sandwich, magnesium transporter, metal transport |
| Biological source | Echinococcus granulosus |
| Total number of polymer chains | 8 |
| Total formula weight | 128735.30 |
| Authors | Shahsavan, A.,Gehring, K. (deposition date: 2023-03-17, release date: 2023-12-13, Last modification date: 2024-11-13) |
| Primary citation | Shahsavan, A.,Lee, E.L.,Illes, K.,Kozlov, G.,Gehring, K. Dimerization of the CNNM extracellular domain. Protein Sci., 33:e4860-e4860, 2024 Cited by 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: 38149326DOI: 10.1002/pro.4860 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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