Published September 22, 2015 | Version public
Journal Article

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

  • 1. ROR icon Aarhus University
  • 2. ROR icon University of Copenhagen
  • 3. ROR icon California Institute of Technology
  • 4. ROR icon Lund University

Abstract

Copper and zinc are micronutrients essential for the function of many enzymes while also being toxic at elevated concentrations. Cu(I)- and Zn(II)-transporting P-type ATPases of subclass 1B are of key importance for the homeostasis of these transition metals, allowing ion transport across cellular membranes at the expense of ATP. Recent biochemical studies and crystal structures have significantly improved our understanding of the transport mechanisms of these proteins, but many details about their structure and function remain 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.

Additional Information

© 2015 American Chemical Society. Received: May 9, 2015; Revised: June 29, 2015; Published: July 1, 2015. This work was supported by The Lundbeck Foundation and the Swedish Research Council. The authors declare no competing financial interest.

Additional details

Identifiers

Eprint ID
61484
DOI
10.1021/acs.biochem.5b00512
Resolver ID
CaltechAUTHORS:20151023-104639212

Funding

Lundbeck Foundation
Swedish Research Council

Dates

Created
2015-10-26
Created from EPrint's datestamp field
Updated
2021-11-10
Created from EPrint's last_modified field