5m8a

Crystal structure of Eremococcus coleocola manganese transporter mutant E129A

spinqualitylabelsall models 5m8a, resolution 3.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5m8a is a 1 chain structure with sequence from Eremococcus coleocola ACS-139-V-Col8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.9Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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