Lumenal loop M672-P707 of the Menkes protein (ATP7A) transfers copper to peptidylglycine monooxygenase.

Journal of the American Chemical Society
Adenike OtoikhianNinian J Blackburn

Abstract

Copper transfer to cuproproteins located in vesicular compartments of the secretory pathway depends on activity of the copper-translocating ATPase (ATP7A), but the mechanism of transfer is largely unexplored. Copper-ATPase ATP7A is unique in having a sequence rich in histidine and methionine residues located on the lumenal side of the membrane. The corresponding fragment binds Cu(I) when expressed as a chimera with a scaffold protein, and mutations or deletions of His and/or Met residues in its sequence inhibit dephosphorylation of the ATPase, a catalytic step associated with copper release. Here we present evidence for a potential role of this lumenal region of ATP7A in copper transfer to cuproenzymes. Both Cu(II) and Cu(I) forms were investigated since the form in which copper is transferred to acceptor proteins is currently unknown. Analysis of Cu(II) using EPR demonstrated that at Cu:P ratios below 1:1 (15)N-substituted protein had Cu(II) bound by 4 His residues, but this coordination changed as the Cu(II) to protein ratio increased toward 2:1. XAS confirmed this coordination via analysis of the intensity of outer-shell scattering from imidazole residues. The Cu(II) complexes could be reduced to their Cu(I) counterparts by ...Continue Reading

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Citations

Aug 22, 2013·Metallomics : Integrated Biometal Science·Vincent BalterFrancis Albarède
Jan 7, 2016·Frontiers in Molecular Neuroscience·Małgorzata LenartowiczLisbeth Birk Møller
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Jun 6, 2021·The FEBS Journal·Nils BäckBetty A Eipper
Aug 15, 2021·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·May T MaungTeresita Padilla-Benavides

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