1994Journal of the American College of NutritionRequires access

Magnesium transport systems: genetics and protein structure (a review).

S K Roof, Michael E. Maguire

Open publisher page 9 citations

Abstract

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.

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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.

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Available abstract

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.

Key concepts: Membrane transport protein, Transporter, Transport protein, Ion transporter, Membrane transport, Magnesium, Biology, Biochemistry

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