Abstract
Copper-transporting ATPase, a member of P-type ATPase family, plays a key role in the homeostasis of cellular copper levels. Here, the backbone assignments of the directly connected N and P domains (292 residues, 31 kDa) of Cu-transporting ATPase in the ligand free and the AMPPCP-bound states are reported in solution. The NMR assignments pave the way for binding and dynamics studies of this enzyme to better understand its function.
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This work was supported by the National Science Foundation (Grant MCB-1360966).
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Meng, D., Bruschweiler-Li, L., Zhang, F. et al. NMR backbone resonance assignments of the N, P domains of CopA, a copper-transporting ATPase, in the apo and ligand bound states. Biomol NMR Assign 9, 129–133 (2015). https://doi.org/10.1007/s12104-014-9558-y
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DOI: https://doi.org/10.1007/s12104-014-9558-y