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Why Is the GMN Motif Conserved in the CorA/Mrs2/Alr1 Superfamily of Magnesium Transport Proteins?
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
2013 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 52, no 28, 4842-4847 p.Article in journal (Refereed) Published
Abstract [en]

Members of the CorA/Mrs2/Alr1 superfamily of transport proteins mediate magnesium uptake in all kingdoms of life. Family members have a low degree of sequence conservation but are characterized by a conserved extracellular loop. While the degree of sequence conservation in the loop deviates to some extent between family members, the GMN family signature motif is always present. Structural and functional data imply that the loop plays a central role in magnesium selectivity, and recent biochemical data suggest it is crucial for stabilizing the pentamer in the magnesium-free (putative open) conformation. In this study, we present a detailed structure-function analysis of the extracellular loop of CorA from Thermotoga maritima, which provides molecular insight into how the loop mediates these two functions. The data show that loop residues outside of the GMN motif can be substituted if they support the pentameric state, but the residues of the GMN motif are intolerant to substitution. We conclude that G(312) is absolutely required for magnesium uptake, M-313 is absolutely required for pentamer integrity in the putative open conformation, and N-314 plays a role in both of these functions. These observations suggest a molecular reason why the GMN motif is conserved throughout the CorA/Mrs2/Alr1 superfamily.

Place, publisher, year, edition, pages
2013. Vol. 52, no 28, 4842-4847 p.
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:su:diva-92924DOI: 10.1021/bi4007397ISI: 000322059400011OAI: diva2:644327
Swedish Research Council


Available from: 2013-08-30 Created: 2013-08-26 Last updated: 2013-08-30Bibliographically approved

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Palombo, IsoldeDaley, Daniel O.
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