Structural and mechanistic basis of proton-coupled metal ion transport in the SLC11/NRAMP family

Ines A. Ehrnstorfer, Cristina Manatschal, Fabian M. Arnold, Juerg Laederach and Raimund Dutzler
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Ines A. Ehrnstorfer: University of Zurich
Cristina Manatschal: University of Zurich
Fabian M. Arnold: University of Zurich
Juerg Laederach: University of Zurich
Raimund Dutzler: University of Zurich

Nature Communications, 2017, vol. 8, issue 1, 1-11

Abstract: Abstract Secondary active transporters of the SLC11/NRAMP family catalyse the uptake of iron and manganese into cells. These proteins are highly conserved across all kingdoms of life and thus likely share a common transport mechanism. Here we describe the structural and functional properties of the prokaryotic SLC11 transporter EcoDMT. Its crystal structure reveals a previously unknown outward-facing state of the protein family. In proteoliposomes EcoDMT mediates proton-coupled uptake of manganese at low micromolar concentrations. Mutants of residues in the transition-metal ion-binding site severely affect transport, whereas a mutation of a conserved histidine located near this site results in metal ion transport that appears uncoupled to proton transport. Combined with previous results, our study defines the conformational changes underlying transition-metal ion transport in the SLC11 family and it provides molecular insight to its coupling to protons.

Date: 2017
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DOI: 10.1038/ncomms14033

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