Structure and function of Cu(I)- and Zn(II)-ATPases

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

  • Oleg Sitsel
  • ,
  • Christina Grønberg, Department of Biomedical Sciences, University of Copenhagen, Denmark
  • Henriette Autzen, Department of Biomedical Sciences, University of Copenhagen, Denmark
  • Kaituo Wang, Department of Biomedical Sciences, University of Copenhagen
  • ,
  • Gabriele Meloni
  • ,
  • Poul Nissen
  • Pontus Gourdon, Department of Biomedical Sciences, University of Copenhagen, Department of Experimental Medical Science, Lund University, Denmark

Copper and zinc are micronutrients essential for the function of many enzymes while also toxic at elevated concentrations. Cu(I)- and Zn(II)-transporting P-type ATPases of subclass 1B are of key importance for homeostasis of these transition metals, allowing ion transport across cellular membranes at the expense of ATP. Recent biochemical studies and crystal structures have significantly increased the understanding of the transport mechanisms of these proteins, but many details about their structure and function remains elusive. Here we compare the Cu(I)- and Zn(II)-ATPases, scrutinizing the molecular differences that allow transport of these two distinct metal types, and discuss possible future directions of research in the field.

Original languageEnglish
JournalBiochemistry
Volume54
Issue37
Pages (from-to)5673-5683
Number of pages11
ISSN0006-2960
DOIs
Publication statusPublished - 1 Jul 2015

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