6m97

Crystal structure of the high-affinity copper transporter Ctr1

spinqualitylabelsall models 6m97, resolution 3.03Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6m97 is a 1 chain structure with sequence from Escherichia coli and Salmo salar. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.03Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C562_ECOLX Electron-transport protein of unknown function.C0HAK2_SALSA Publication Abstract from PubMed Copper (Cu) is an essential trace element for growth and development and abnormal Cu levels are associated with anemia, metabolic disease and cancer. Evolutionarily conserved from fungi to humans, the high-affinity Cu(+) transporter Ctr1 is crucial for both dietary Cu uptake and peripheral distribution, yet the mechanisms for selective permeation of potentially toxic Cu(+) ions across cell membranes are unknown. Here we present X-ray crystal structures of Ctr1 from Salmo salar in both Cu(+)-free and Cu(+)-bound states, revealing a homo-trimeric Cu(+)-selective ion channel-like architecture. Two layers of methionine triads form a selectivity filter, coordinating two bound Cu(+) ions close to the extracellular entrance. These structures, together with Ctr1 functional characterization, provide a high resolution picture to understand Cu(+) import across cellular membranes and suggest therapeutic opportunities for intervention in diseases characterized by inappropriate Cu accumulation. X-ray structures of the high-affinity copper transporter Ctr1.,Ren F, Logeman BL, Zhang X, Liu Y, Thiele DJ, Yuan P Nat Commun. 2019 Mar 27;10(1):1386. doi: 10.1038/s41467-019-09376-7. PMID:30918258 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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