期刊
SCIENCE ADVANCES
卷 7, 期 7, 页码 -出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.abe6140
关键词
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资金
- Ministry of Science and Technology of China (National Key R&D Program of China) [2016YFA0502800]
- National Natural Science Foundation of China [31850410466, 32071234]
- Opening Project of State Key Laboratory of Genetic Engineering [SKLGE-1813]
- Innovative Research Team of High-Level Local University in Shanghai
- key laboratory program of the Education Commission of Shanghai Municipality [ZDSYS14005]
- Japan Society for the Promotion of Science [JP26111007, JP17H04041, JP20H03515, JP20K07312, JP20H05508, JP17K19396]
CNNM/CorC family proteins play a crucial role in Mg2+ transport in organisms. Structural and functional analyses provide important clues for the Mg2+ export activity of CorC.
The CNNM/CorC family proteins are Mg2+ 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 Mg2+ and genetic disorders. Here, we determined the crystal structure of the Mg2+-bound CorC TM domain dimer. Each protomer has a single Mg2+ binding site with a fully dehydrated Mg2+ ion. The residues at the Mg2+ 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 Mg2+ export activity of CorC.
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