6M97
Crystal structure of the high-affinity copper transporter Ctr1
Summary for 6M97
| Entry DOI | 10.2210/pdb6m97/pdb |
| Descriptor | Chimera protein of High affinity copper uptake protein 1 and Soluble cytochrome b562, HEXATANTALUM DODECABROMIDE, ZINC ION (3 entities in total) |
| Functional Keywords | membrane proteins, ion transporters, ion channels., transport protein |
| Biological source | Salmo salar (Atlantic salmon) More |
| Total number of polymer chains | 1 |
| Total formula weight | 30426.95 |
| Authors | |
| Primary citation | Ren, F.,Logeman, B.L.,Zhang, X.,Liu, Y.,Thiele, D.J.,Yuan, P. X-ray structures of the high-affinity copper transporter Ctr1. Nat Commun, 10:1386-1386, 2019 Cited by PubMed Abstract: 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. PubMed: 30918258DOI: 10.1038/s41467-019-09376-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.03 Å) |
Structure validation
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