X-ray structures of the high-affinity copper transporter Ctr1

• DOI: 10.1038/s41467-019-09376-7
• Publication Date: 2019-03-27T16:49:55Z
• Authors: Feifei Ren; Brandon L. Logeman; Xiaohui Zhang; Yongjian Liu; Dennis J. Thiele; Peng Yuan
• Keywords: 0301 basic medicine; 0303 health sciences; Ion Transport; Science; Q; Cell Membrane; Salmo salar; Biological Transport; Crystallography, X-Ray; Article; 3. Good health; 03 medical and health sciences; Animals; Cation Transport Proteins; Copper; Copper Transporter 1

Abstract Copper (Cu) is an essential trace element for growth and development abnormal Cu levels are associated with anemia, metabolic disease cancer. Evolutionarily conserved from fungi to humans, the high-affinity + transporter Ctr1 crucial both dietary uptake peripheral distribution, yet mechanisms selective permeation of potentially toxic ions across cell membranes unknown. Here we present X-ray crystal structures Salmo salar in -free -bound states, revealing a homo-trimeric -selective ion channel-like architecture. Two layers methionine triads form selectivity filter, coordinating two bound close extracellular entrance. These structures, together functional characterization, provide high resolution picture understand import cellular suggest therapeutic opportunities intervention diseases characterized by inappropriate accumulation.