Structural highlights
Function
E4KPW4_9LACT H(+)-stimulated, divalent metal cation uptake system.[HAMAP-Rule:MF_00221]
Publication Abstract from PubMed
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.
Structural and mechanistic basis of proton-coupled metal ion transport in the SLC11/NRAMP family.,Ehrnstorfer IA, Manatschal C, Arnold FM, Laederach J, Dutzler R Nat Commun. 2017 Jan 6;8:14033. doi: 10.1038/ncomms14033. PMID:28059071[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ehrnstorfer IA, Manatschal C, Arnold FM, Laederach J, Dutzler R. Structural and mechanistic basis of proton-coupled metal ion transport in the SLC11/NRAMP family. Nat Commun. 2017 Jan 6;8:14033. doi: 10.1038/ncomms14033. PMID:28059071 doi:http://dx.doi.org/10.1038/ncomms14033
