National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS)
NS109307
United States
National Institutes of Health/National Cancer Institute (NIH/NCI)
P30 CA008748
United States
Citation
Journal: Sci Adv / Year: 2022 Title: Structure of the Wilson disease copper transporter ATP7B. Authors: Ryan M Bitter / SeCheol Oh / Zengqin Deng / Suhaila Rahman / Richard K Hite / Peng Yuan / Abstract: ATP7A and ATP7B, two homologous copper-transporting P1B-type ATPases, play crucial roles in cellular copper homeostasis, and mutations cause Menkes and Wilson diseases, respectively. ATP7A/B contains ...ATP7A and ATP7B, two homologous copper-transporting P1B-type ATPases, play crucial roles in cellular copper homeostasis, and mutations cause Menkes and Wilson diseases, respectively. ATP7A/B contains a P-type ATPase core consisting of a membrane transport domain and three cytoplasmic domains, the A, P, and N domains, and a unique amino terminus comprising six consecutive metal-binding domains. Here, we present a cryo-electron microscopy structure of frog ATP7B in a copper-free state. Interacting with both the A and P domains, the metal-binding domains are poised to exert copper-dependent regulation of ATP hydrolysis coupled to transmembrane copper transport. A ring of negatively charged residues lines the cytoplasmic copper entrance that is presumably gated by a conserved basic residue sitting at the center. Within the membrane, a network of copper-coordinating ligands delineates a stepwise copper transport pathway. This work provides the first glimpse into the structure and function of ATP7 proteins and facilitates understanding of disease mechanisms and development of rational therapies.
History
Deposition
Oct 12, 2021
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Header (metadata) release
Mar 16, 2022
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Map release
Mar 16, 2022
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Update
Mar 16, 2022
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Current status
Mar 16, 2022
Processing site: RCSB / Status: Released
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