Crystal structure of a copper-transporting PIB-type ATPase

Pontus Gourdon, Xiang-Yu Liu, Tina Skjørringe, J. Preben Morth, Lisbeth Birk Møller (), Bjørn Panyella Pedersen and Poul Nissen ()
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Pontus Gourdon: Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C
Xiang-Yu Liu: Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C
Tina Skjørringe: Center for Applied Human Molecular Genetics, Kennedy Center, Gl. Landevej 7
J. Preben Morth: Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C
Lisbeth Birk Møller: Center for Applied Human Molecular Genetics, Kennedy Center, Gl. Landevej 7
Bjørn Panyella Pedersen: Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C
Poul Nissen: Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C

Nature, 2011, vol. 475, issue 7354, 59-64

Abstract: Abstract Heavy-metal homeostasis and detoxification is crucial for cell viability. P-type ATPases of the class IB (PIB) are essential in these processes, actively extruding heavy metals from the cytoplasm of cells. Here we present the structure of a PIB-ATPase, a Legionella pneumophila CopA Cu+-ATPase, in a copper-free form, as determined by X-ray crystallography at 3.2 Å resolution. The structure indicates a three-stage copper transport pathway involving several conserved residues. A PIB-specific transmembrane helix kinks at a double-glycine motif displaying an amphipathic helix that lines a putative copper entry point at the intracellular interface. Comparisons to Ca2+-ATPase suggest an ATPase-coupled copper release mechanism from the binding sites in the membrane via an extracellular exit site. The structure also provides a framework to analyse missense mutations in the human ATP7A and ATP7B proteins associated with Menkes’ and Wilson’s diseases.

Date: 2011
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DOI: 10.1038/nature10191

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