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

Sitsel, Oleg; Gronberg, Christina; Autzen, Henriette Elisabeth; Wang, Kaituo; Meloni, Gabriele; Nissen, Poul and Gourdon, Pontus LU (2015) In Biochemistry 54(37). p.5673-5683
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.
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemistry
volume
54
issue
37
pages
5673 - 5683
publisher
The American Chemical Society
external identifiers
  • wos:000361935200003
  • scopus:84942083510
ISSN
0006-2960
DOI
10.1021/acs.biochem.5b00512
language
English
LU publication?
yes
id
d587feeb-578a-4400-847b-b90309f1d381 (old id 8225172)
date added to LUP
2015-12-01 12:01:38
date last changed
2017-10-29 03:17:39
@article{d587feeb-578a-4400-847b-b90309f1d381,
  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.},
  author       = {Sitsel, Oleg and Gronberg, Christina and Autzen, Henriette Elisabeth and Wang, Kaituo and Meloni, Gabriele and Nissen, Poul and Gourdon, Pontus},
  issn         = {0006-2960},
  language     = {eng},
  number       = {37},
  pages        = {5673--5683},
  publisher    = {The American Chemical Society},
  series       = {Biochemistry},
  title        = {Structure and Function of Cu(I)- and Zn(II)-ATPases},
  url          = {http://dx.doi.org/10.1021/acs.biochem.5b00512},
  volume       = {54},
  year         = {2015},
}