5M8A

Crystal structure of Eremococcus coleocola manganese transporter mutant E129A

Summary for 5M8A

• Entry DOI: 10.2210/pdb5m8a/pdb
• Descriptor: Divalent metal cation transporter MntH (1 entity in total)
• Functional Keywords: transport protein
• Biological source: Eremococcus coleocola ACS-139-V-Col8
• Cellular location: Cell membrane ; Multi-pass membrane protein : E4KPW4
• Total number of polymer chains: 1
• Total formula weight: 56570.52

Authors

Manatschal, C.,Ehrnstorfer, I.A.,Arnold, F.M.,Laederach, J.,Dutzler, R. (deposition date: 2016-10-28, release date: 2017-01-11, Last modification date: 2024-01-17)

Primary citation

Ehrnstorfer, I.A.,Manatschal, C.,Arnold, F.M.,Laederach, J.,Dutzler, R.
Structural and mechanistic basis of proton-coupled metal ion transport in the SLC11/NRAMP family.
Nat Commun, 8:14033-14033, 2017

PubMed 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.

PubMed: 28059071
DOI: 10.1038/ncomms14033

Experimental method

X-RAY DIFFRACTION (3.9 Å)