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Critical role of γ-phosphate in structural transition of Na,K-ATPase upon ATP binding

Active transport of sodium and potassium ions by Na,K-ATPase is accompanied by the enzyme conformational transition between E1 and E2 states. ATP and ADP bind to Na,K-ATPase in the E1 conformation with similar affinity but the properties of enzyme in complexes with these nucleotides are different. W...

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Autores principales: Petrushanko, Irina Yu., Mitkevich, Vladimir A., Anashkina, Anastasia A., Klimanova, Elizaveta A., Dergousova, Elena A., Lopina, Olga D., Makarov, Alexander A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4044624/
https://www.ncbi.nlm.nih.gov/pubmed/24893715
http://dx.doi.org/10.1038/srep05165
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author Petrushanko, Irina Yu.
Mitkevich, Vladimir A.
Anashkina, Anastasia A.
Klimanova, Elizaveta A.
Dergousova, Elena A.
Lopina, Olga D.
Makarov, Alexander A.
author_facet Petrushanko, Irina Yu.
Mitkevich, Vladimir A.
Anashkina, Anastasia A.
Klimanova, Elizaveta A.
Dergousova, Elena A.
Lopina, Olga D.
Makarov, Alexander A.
author_sort Petrushanko, Irina Yu.
collection PubMed
description Active transport of sodium and potassium ions by Na,K-ATPase is accompanied by the enzyme conformational transition between E1 and E2 states. ATP and ADP bind to Na,K-ATPase in the E1 conformation with similar affinity but the properties of enzyme in complexes with these nucleotides are different. We have studied thermodynamics of Na,K-ATPase binding with adenine nucleotides at different temperatures using isothermal titration calorimetry. Our data indicate that β-phosphate is involved in complex formation by increasing the affinity of adenine nucleotides to Na,K-ATPase by an order of magnitude, while γ-phosphate does not affect it. ATP binding to Na,K-ATPase in contrast to ADP binding generates a structural transition in the enzyme, which is consistent with the movement of a significant portion of the surface area to a solvent-protected state. We propose that ATP binding leads to convergence of the nucleotide-binding and phosphorylation domains transferring the enzyme from the “E1-open” to “E1-closed” conformation ready for phosphorylation.
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spelling pubmed-40446242014-06-12 Critical role of γ-phosphate in structural transition of Na,K-ATPase upon ATP binding Petrushanko, Irina Yu. Mitkevich, Vladimir A. Anashkina, Anastasia A. Klimanova, Elizaveta A. Dergousova, Elena A. Lopina, Olga D. Makarov, Alexander A. Sci Rep Article Active transport of sodium and potassium ions by Na,K-ATPase is accompanied by the enzyme conformational transition between E1 and E2 states. ATP and ADP bind to Na,K-ATPase in the E1 conformation with similar affinity but the properties of enzyme in complexes with these nucleotides are different. We have studied thermodynamics of Na,K-ATPase binding with adenine nucleotides at different temperatures using isothermal titration calorimetry. Our data indicate that β-phosphate is involved in complex formation by increasing the affinity of adenine nucleotides to Na,K-ATPase by an order of magnitude, while γ-phosphate does not affect it. ATP binding to Na,K-ATPase in contrast to ADP binding generates a structural transition in the enzyme, which is consistent with the movement of a significant portion of the surface area to a solvent-protected state. We propose that ATP binding leads to convergence of the nucleotide-binding and phosphorylation domains transferring the enzyme from the “E1-open” to “E1-closed” conformation ready for phosphorylation. Nature Publishing Group 2014-06-04 /pmc/articles/PMC4044624/ /pubmed/24893715 http://dx.doi.org/10.1038/srep05165 Text en Copyright © 2014, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by-nc-sa/3.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. The images in this article are included in the article's Creative Commons license, unless indicated otherwise in the image credit; if the image is not included under the Creative Commons license, users will need to obtain permission from the license holder in order to reproduce the image. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/
spellingShingle Article
Petrushanko, Irina Yu.
Mitkevich, Vladimir A.
Anashkina, Anastasia A.
Klimanova, Elizaveta A.
Dergousova, Elena A.
Lopina, Olga D.
Makarov, Alexander A.
Critical role of γ-phosphate in structural transition of Na,K-ATPase upon ATP binding
title Critical role of γ-phosphate in structural transition of Na,K-ATPase upon ATP binding
title_full Critical role of γ-phosphate in structural transition of Na,K-ATPase upon ATP binding
title_fullStr Critical role of γ-phosphate in structural transition of Na,K-ATPase upon ATP binding
title_full_unstemmed Critical role of γ-phosphate in structural transition of Na,K-ATPase upon ATP binding
title_short Critical role of γ-phosphate in structural transition of Na,K-ATPase upon ATP binding
title_sort critical role of γ-phosphate in structural transition of na,k-atpase upon atp binding
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4044624/
https://www.ncbi.nlm.nih.gov/pubmed/24893715
http://dx.doi.org/10.1038/srep05165
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