7CFG
Structure of the transmembrane domain of the bacterial CNNM/CorC family Mg2+ transporter in complex with Mg2+
Summary for 7CFG
| Entry DOI | 10.2210/pdb7cfg/pdb |
| Descriptor | Hemolysin, ZINC ION, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | transporter, transport protein |
| Biological source | Thermus parvatiensis |
| Total number of polymer chains | 1 |
| Total formula weight | 19410.62 |
| Authors | Huang, Y.,Jin, F.,Hattori, M. (deposition date: 2020-06-25, release date: 2021-02-24, Last modification date: 2024-03-27) |
| Primary citation | Huang, Y.,Jin, F.,Funato, Y.,Xu, Z.,Zhu, W.,Wang, J.,Sun, M.,Zhao, Y.,Yu, Y.,Miki, H.,Hattori, M. Structural basis for the Mg 2+ recognition and regulation of the CorC Mg 2+ transporter. Sci Adv, 7:-, 2021 Cited by PubMed Abstract: The CNNM/CorC family proteins are Mg transporters that are widely distributed in all domains of life. In bacteria, CorC has been implicated in the survival of pathogenic microorganisms. In humans, CNNM proteins are involved in various biological events, such as body absorption/reabsorption of Mg and genetic disorders. Here, we determined the crystal structure of the Mg-bound CorC TM domain dimer. Each protomer has a single Mg binding site with a fully dehydrated Mg ion. The residues at the Mg binding site are strictly conserved in both human CNNM2 and CNNM4, and many of these residues are associated with genetic diseases. Furthermore, we determined the structures of the CorC cytoplasmic region containing its regulatory ATP-binding domain. A combination of structural and functional analyses not only revealed the potential interface between the TM and cytoplasmic domains but also showed that ATP binding is important for the Mg export activity of CorC. PubMed: 33568487DOI: 10.1126/sciadv.abe6140 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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