7CFF

Structure of the thermostabilized transmembrane domain of the bacterial CNNM/CorC family Mg2+ transporter in complex with Mg2+

7CFF の概要

• エントリーDOI: 10.2210/pdb7cff/pdb
• 分子名称: Hemolysin, ZINC ION, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: transporter, transport protein
• 由来する生物種: Thermus parvatiensis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19691.95

構造登録者

Huang, Y.,Jin, F.,Hattori, M. (登録日: 2020-06-25, 公開日: 2021-02-24, 最終更新日: 2024-03-27)

主引用文献

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

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: 33568487
DOI: 10.1126/sciadv.abe6140

実験手法

X-RAY DIFFRACTION (2 Å)