Crystal structure of the CorA Mg2+ transporter

Vladimir V. Lunin, Elena Dobrovetsky, Galina Khutoreskaya, Rongguang Zhang, Andrzej Joachimiak, Declan A. Doyle, Alexey Bochkarev, Michael E. Maguire (), Aled M. Edwards () and Christopher M. Koth
Additional contact information
Vladimir V. Lunin: Department of Medical Biophysics
Elena Dobrovetsky: Banting and Best Department of Medical Research
Galina Khutoreskaya: Banting and Best Department of Medical Research
Rongguang Zhang: Argonne National Laboratory
Andrzej Joachimiak: Argonne National Laboratory
Declan A. Doyle: Botnar Research Centre
Alexey Bochkarev: Banting and Best Department of Medical Research
Michael E. Maguire: Case Western Reserve University
Aled M. Edwards: Department of Medical Biophysics
Christopher M. Koth: Banting and Best Department of Medical Research

Nature, 2006, vol. 440, issue 7085, 833-837

Abstract: Magnesium ally The transport mechanisms of most major biological ions have been determined in detail, apart from magnesium. CorA-type transporters are the main Mg2+ uptake system in most prokaryotes and in mitochondria. Now the crystal structure of bacterial CorA in the closed state has been determined. The transporter is a funnel-shaped homopentamer; the presence of a conserved Mg2+ binding site in the cytoplasmic domain suggests a mechanism to link the gating of the pore to the intracellular concentration of the ion.

Date: 2006
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DOI: 10.1038/nature04642

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