当前位置: X-MOL 学术Structure › 论文详情
Mg2+-ATP Sensing in CNNM, a Putative Magnesium Transporter
Structure ( IF 4.576 ) Pub Date : 2019-12-18 , DOI: 10.1016/j.str.2019.11.016
Yu Seby Chen; Guennadi Kozlov; Rayan Fakih; Meng Yang; Zhidian Zhang; Evgenii L. Kovrigin; Kalle Gehring

The family of cystathionine-β-synthase (CBS)-pair domain divalent metal cation transport mediators (CNNMs) is composed of four integral membrane proteins associated with Mg2+ transport. Structurally, CNNMs contain large cytosolic regions composed of a CBS-pair and a cyclic nucleotide-binding homology (CNBH) domain. How these regulate Mg2+ transport activity is unknown. Here, we determined the crystal structures of cytosolic fragments in two conformations: Mg2+-ATP-analog bound and ligand free. The structures reveal open and closed conformations with functionally important contacts not observed in structures of the individual domains. We also identified a second Mg2+-binding region in the CBS-pair domain and a different dimerization interface for the CNBH domain. Analytical ultracentrifugation and isothermal titration calorimetry experiments revealed a tight correlation between Mg2+-ATP binding and protein dimerization. Mutations that blocked either function prevented cellular Mg2+ efflux activity. The results suggest Mg2+ efflux is regulated by conformational changes associated with Mg2+-ATP binding to CNNM CBS-pair domains.
更新日期:2019-12-19

 

全部期刊列表>>
Springer Nature 2019高下载量文章和章节
化学/材料学中国作者研究精选
《科学报告》最新环境科学研究
ACS材料视界
自然科研论文编辑服务
中南大学国家杰青杨华明
剑桥大学-
中南大学
材料化学和生物传感方向博士后招聘
课题组网站
X-MOL
北京大学分子工程苏南研究院
华东师范大学分子机器及功能材料
中山大学化学工程与技术学院
试剂库存
天合科研
down
wechat
bug