Litcius/Paper detail

Structural and functional properties of a magnesium transporter of the SLC11/NRAMP family

Karthik Ramanadane, Monique S Straub, Raimund Dutzler, Cristina Manatschal

2022eLife19 citationsDOIOpen Access PDF

Abstract

Members of the ubiquitous SLC11/NRAMP family catalyze the uptake of divalent transition metal ions into cells. They have evolved to efficiently select these trace elements from a large pool of Ca 2+ and Mg 2+ , which are both orders of magnitude more abundant, and to concentrate them in the cytoplasm aided by the cotransport of H + serving as energy source. In the present study, we have characterized a member of a distant clade of the family found in prokaryotes, termed NRMTs, that were proposed to function as transporters of Mg 2+ . The protein transports Mg 2+ and Mn 2+ but not Ca 2+ by a mechanism that is not coupled to H + . Structures determined by cryo-EM and X-ray crystallography revealed a generally similar protein architecture compared to classical NRAMPs, with a restructured ion binding site whose increased volume provides suitable interactions with ions that likely have retained much of their hydration shell.

Topics & Concepts

ChemistryCotransporterDivalentTransporterCytoplasmBiophysicsFunction (biology)CrystallographyProtein structureBiochemistryIonMagnesiumBinding siteProtein familyPlasma protein bindingMembrane transport proteinSymporterTransport proteinIon transporterPeptide sequenceProtein domainMetal ions in aqueous solutionSolute carrier familyMechanism (biology)Protein foldingPeptideTransmembrane domainMagnesium in Health and DiseaseIon Transport and Channel RegulationAluminum toxicity and tolerance in plants and animals