Magnesium transport systems: genetics and protein structure (a review).
Magnesium is unique among biological cations. Its volume change from hydrated cation to atomic ion is over an order of magnitude larger than that of any other biological cation. This volume change presents particular problems for a magnesium transport system and suggests that these systems may be significantly different from other classes of ion transport systems. Detailed study of Mg2+ transport in complex organisms is limited by severe technical problems. However, molecular genetic techniques have enabled the isolation of three Mg2+ transport systems from the Gram-negative bacterium Salmonella typhimurium. The MgtA and MgtB transport systems are members of the P-type ATPase superfamily of transporters but possess unique characteristics among members of this family. The CorA transport protein is the first member of an entirely new class of transport proteins. In addition, another completely new family of Mg2+ transport proteins have been identified that is present in both Gram-negative and Gram-positive bacteria. Characterization of these transporters should provide substantial insight into Mg2+ transport and cellular Mg2+ homeostasis.
Department of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, OH 44106-4965.
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Maguire
D000251:Adenosine Triphosphatases / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins; D001692:Biological Transport; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D027682:Cation Transport Proteins; D004926:Escherichia coli; D008274:Magnesium / Q000737:chemistry / Q000378:metabolism*; D012486:Salmonella typhimurium
D001426:Bacterial Proteins; D002352:Carrier Proteins; D027682:Cation Transport Proteins; C072716:CorA protein, Salmonella; D000251:Adenosine Triphosphatases; D008274:Magnesium