ATP-dependent modulation of MgtE in Mg2+ homeostasis View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-12

AUTHORS

Atsuhiro Tomita, Mingfeng Zhang, Fei Jin, Wenhui Zhuang, Hironori Takeda, Tatsuro Maruyama, Masanori Osawa, Ken-ichi Hashimoto, Hisashi Kawasaki, Koichi Ito, Naoshi Dohmae, Ryuichiro Ishitani, Ichio Shimada, Zhiqiang Yan, Motoyuki Hattori, Osamu Nureki

ABSTRACT

Magnesium is an essential ion for numerous physiological processes. MgtE is a Mg2+ selective channel involved in the maintenance of intracellular Mg2+ homeostasis, whose gating is regulated by intracellular Mg2+ levels. Here, we report that ATP binds to MgtE, regulating its Mg2+-dependent gating. Crystal structures of MgtE-ATP complex show that ATP binds to the intracellular CBS domain of MgtE. Functional studies support that ATP binding to MgtE enhances the intracellular domain affinity for Mg2+ within physiological concentrations of this divalent cation, enabling MgtE to function as an in vivo Mg2+ sensor. ATP dissociation from MgtE upregulates Mg2+ influx at both high and low intracellular Mg2+ concentrations. Using site-directed mutagenesis and structure based-electrophysiological and biochemical analyses, we identify key residues and main structural changes involved in the process. This work provides the molecular basis of ATP-dependent modulation of MgtE in Mg2+ homeostasis.MgtE is an Mg2+ transporter involved in Mg2+ homeostasis. Here, the authors report that ATP regulates the Mg+2-dependent gating of MgtE and use X-ray crystallography combined with functional studies to propose the molecular mechanisms involved in this process. More... »

PAGES

148

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41467-017-00082-w

DOI

http://dx.doi.org/10.1038/s41467-017-00082-w

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1090836284

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/28747715


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