Advanced

On allosteric modulation of P-type Cu(+)-ATPases

Mattle, Daniel; Sitsel, Oleg; Autzen, Henriette Elisabeth; Meloni, Gabriele; Gourdon, Pontus LU and Nissen, Poul (2013) In Journal of Molecular Biology 425(13). p.308-2299
Abstract

P-type ATPases perform active transport of various compounds across biological membranes and are crucial for ion homeostasis and the asymmetric composition of lipid bilayers. Although their functional cycle share principles of phosphoenzyme intermediates, P-type ATPases also show subclass-specific sequence motifs and structural elements that are linked to transport specificity and mechanistic modulation. Here we provide an overview of the Cu(+)-transporting ATPases (of subclass PIB) and compare them to the well-studied sarco(endo)plasmic reticulum Ca(2+)-ATPase (of subclass PIIA). Cu(+) ions in the cell are delivered by soluble chaperones to Cu(+)-ATPases, which expose a putative "docking platform" at the intracellular interface.... (More)

P-type ATPases perform active transport of various compounds across biological membranes and are crucial for ion homeostasis and the asymmetric composition of lipid bilayers. Although their functional cycle share principles of phosphoenzyme intermediates, P-type ATPases also show subclass-specific sequence motifs and structural elements that are linked to transport specificity and mechanistic modulation. Here we provide an overview of the Cu(+)-transporting ATPases (of subclass PIB) and compare them to the well-studied sarco(endo)plasmic reticulum Ca(2+)-ATPase (of subclass PIIA). Cu(+) ions in the cell are delivered by soluble chaperones to Cu(+)-ATPases, which expose a putative "docking platform" at the intracellular interface. Cu(+)-ATPases also contain heavy-metal binding domains providing a basis for allosteric control of pump activity. Database analysis of Cu(+) ligating residues questions a two-site model of intramembranous Cu(+) binding, and we suggest an alternative role for the proposed second site in copper translocation and proton exchange. The class-specific features demonstrate that topological diversity in P-type ATPases may tune a general energy coupling scheme to the translocation of compounds with remarkably different properties.

(Less)
Please use this url to cite or link to this publication:
author
publishing date
type
Contribution to journal
publication status
published
keywords
Adenosine Triphosphatases, Allosteric Regulation, Binding Sites, Cation Transport Proteins, Crystallography, X-Ray, Ion Transport, Models, Biological, Models, Molecular, Molecular Dynamics Simulation, Protein Conformation, Journal Article, Research Support, Non-U.S. Gov't, Review
in
Journal of Molecular Biology
volume
425
issue
13
pages
308 - 2299
publisher
Elsevier
external identifiers
  • scopus:84879126056
ISSN
1089-8638
DOI
10.1016/j.jmb.2013.03.008
language
English
LU publication?
no
id
d26844ab-45ad-4206-94d2-fdf115a002ec
date added to LUP
2017-04-29 15:31:02
date last changed
2018-01-14 04:31:59
@article{d26844ab-45ad-4206-94d2-fdf115a002ec,
  abstract     = {<p>P-type ATPases perform active transport of various compounds across biological membranes and are crucial for ion homeostasis and the asymmetric composition of lipid bilayers. Although their functional cycle share principles of phosphoenzyme intermediates, P-type ATPases also show subclass-specific sequence motifs and structural elements that are linked to transport specificity and mechanistic modulation. Here we provide an overview of the Cu(+)-transporting ATPases (of subclass PIB) and compare them to the well-studied sarco(endo)plasmic reticulum Ca(2+)-ATPase (of subclass PIIA). Cu(+) ions in the cell are delivered by soluble chaperones to Cu(+)-ATPases, which expose a putative "docking platform" at the intracellular interface. Cu(+)-ATPases also contain heavy-metal binding domains providing a basis for allosteric control of pump activity. Database analysis of Cu(+) ligating residues questions a two-site model of intramembranous Cu(+) binding, and we suggest an alternative role for the proposed second site in copper translocation and proton exchange. The class-specific features demonstrate that topological diversity in P-type ATPases may tune a general energy coupling scheme to the translocation of compounds with remarkably different properties.</p>},
  author       = {Mattle, Daniel and Sitsel, Oleg and Autzen, Henriette Elisabeth and Meloni, Gabriele and Gourdon, Pontus and Nissen, Poul},
  issn         = {1089-8638},
  keyword      = {Adenosine Triphosphatases,Allosteric Regulation,Binding Sites,Cation Transport Proteins,Crystallography, X-Ray,Ion Transport,Models, Biological,Models, Molecular,Molecular Dynamics Simulation,Protein Conformation,Journal Article,Research Support, Non-U.S. Gov't,Review},
  language     = {eng},
  month        = {07},
  number       = {13},
  pages        = {308--2299},
  publisher    = {Elsevier},
  series       = {Journal of Molecular Biology},
  title        = {On allosteric modulation of P-type Cu(+)-ATPases},
  url          = {http://dx.doi.org/10.1016/j.jmb.2013.03.008},
  volume       = {425},
  year         = {2013},
}