6M97

Crystal structure of the high-affinity copper transporter Ctr1

6M97 の概要

• エントリーDOI: 10.2210/pdb6m97/pdb
• 分子名称: Chimera protein of High affinity copper uptake protein 1 and Soluble cytochrome b562, HEXATANTALUM DODECABROMIDE, ZINC ION (3 entities in total)
• 機能のキーワード: membrane proteins, ion transporters, ion channels., transport protein
• 由来する生物種: Salmo salar (Atlantic salmon); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30426.95

構造登録者

Ren, F.,Yuan, P. (登録日: 2018-08-22, 公開日: 2019-04-03, 最終更新日: 2024-03-13)

主引用文献

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

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: 30918258
DOI: 10.1038/s41467-019-09376-7

実験手法

X-RAY DIFFRACTION (3.03 Å)