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    Rights statement: This document is the Accepted Manuscript version of a Published Work that appeared in final form in Biochemistry, copyright ©2015 American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://pubs.acs.org/doi/10.1021/acs.biochem.5b00893

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Long-range effects of Na+ binding in Na,K-ATPase reported by ATP

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Long-range effects of Na+ binding in Na,K-ATPase reported by ATP. / Middleton, David Andrew; Fedosova, Natalya U.; Esmann, Mikael.

In: Biochemistry, Vol. 54, No. 47, 01.12.2015, p. 7041-7047.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Middleton, DA, Fedosova, NU & Esmann, M 2015, 'Long-range effects of Na+ binding in Na,K-ATPase reported by ATP', Biochemistry, vol. 54, no. 47, pp. 7041-7047. https://doi.org/10.1021/acs.biochem.5b00893

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Middleton, David Andrew ; Fedosova, Natalya U. ; Esmann, Mikael. / Long-range effects of Na+ binding in Na,K-ATPase reported by ATP. In: Biochemistry. 2015 ; Vol. 54, No. 47. pp. 7041-7047.

Bibtex

@article{de146c29231e47d58be066d6df23655e,
title = "Long-range effects of Na+ binding in Na,K-ATPase reported by ATP",
abstract = "This paper addresses the question of long-range interactions between the intramembranous cation binding sites and the cytoplasmic nucleotide binding site of the ubiquitous ion-transporting Na,K-ATPase using 13C cross-polarization magic-angle spinning (CP-MAS) solid-state NMR. High affinity ATP binding is induced by the presence of Na+ as well as of Na-like substances such as Tris+, and these ions are equally efficient promoters of nucleotide binding. CP-MAS analysis of bound ATP with Na,K-ATPase purified from pig kidney membranes reveals subtle differences in the nucleotide interactions within the nucleotide site depending on whether Na+ or Tris+ are used to induce binding. Differences in chemical shifts for ATP carbon atoms C1´ and C5´ observed in the presence of Na+ or Tris+ suggest alterations in the residues surrounding the bound nucleotide, hydrogen bonding and/or conformation of the ribose ring. This is taken as evidence for a long-distance communication between the Na+-filled ion sites in the membrane interior and the nucleotide binding site in the cytoplasmic domain and reflects the first conformational change ultimately leading to phosphorylation of the enzyme. Stopped-flow fluorescence measurements with the nucleotide analog eosin show that the dissociation rate constant for eosin is larger in Tris+ than in Na+, giving kinetic evidence for the difference in structural effects of Na+ and Tris+. According to the recent crystal structure of the E1•AlF4 -•ADP•3Na+-form the coupling between the ion binding sites and the nucleotide side is mediated by - among others - the M5-helix.",
author = "Middleton, {David Andrew} and Fedosova, {Natalya U.} and Mikael Esmann",
note = "This document is the Accepted Manuscript version of a Published Work that appeared in final form in Biochemistry, copyright {\textcopyright}2015 American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://pubs.acs.org/doi/10.1021/acs.biochem.5b00893",
year = "2015",
month = dec,
day = "1",
doi = "10.1021/acs.biochem.5b00893",
language = "English",
volume = "54",
pages = "7041--7047",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "47",

}

RIS

TY - JOUR

T1 - Long-range effects of Na+ binding in Na,K-ATPase reported by ATP

AU - Middleton, David Andrew

AU - Fedosova, Natalya U.

AU - Esmann, Mikael

N1 - This document is the Accepted Manuscript version of a Published Work that appeared in final form in Biochemistry, copyright ©2015 American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://pubs.acs.org/doi/10.1021/acs.biochem.5b00893

PY - 2015/12/1

Y1 - 2015/12/1

N2 - This paper addresses the question of long-range interactions between the intramembranous cation binding sites and the cytoplasmic nucleotide binding site of the ubiquitous ion-transporting Na,K-ATPase using 13C cross-polarization magic-angle spinning (CP-MAS) solid-state NMR. High affinity ATP binding is induced by the presence of Na+ as well as of Na-like substances such as Tris+, and these ions are equally efficient promoters of nucleotide binding. CP-MAS analysis of bound ATP with Na,K-ATPase purified from pig kidney membranes reveals subtle differences in the nucleotide interactions within the nucleotide site depending on whether Na+ or Tris+ are used to induce binding. Differences in chemical shifts for ATP carbon atoms C1´ and C5´ observed in the presence of Na+ or Tris+ suggest alterations in the residues surrounding the bound nucleotide, hydrogen bonding and/or conformation of the ribose ring. This is taken as evidence for a long-distance communication between the Na+-filled ion sites in the membrane interior and the nucleotide binding site in the cytoplasmic domain and reflects the first conformational change ultimately leading to phosphorylation of the enzyme. Stopped-flow fluorescence measurements with the nucleotide analog eosin show that the dissociation rate constant for eosin is larger in Tris+ than in Na+, giving kinetic evidence for the difference in structural effects of Na+ and Tris+. According to the recent crystal structure of the E1•AlF4 -•ADP•3Na+-form the coupling between the ion binding sites and the nucleotide side is mediated by - among others - the M5-helix.

AB - This paper addresses the question of long-range interactions between the intramembranous cation binding sites and the cytoplasmic nucleotide binding site of the ubiquitous ion-transporting Na,K-ATPase using 13C cross-polarization magic-angle spinning (CP-MAS) solid-state NMR. High affinity ATP binding is induced by the presence of Na+ as well as of Na-like substances such as Tris+, and these ions are equally efficient promoters of nucleotide binding. CP-MAS analysis of bound ATP with Na,K-ATPase purified from pig kidney membranes reveals subtle differences in the nucleotide interactions within the nucleotide site depending on whether Na+ or Tris+ are used to induce binding. Differences in chemical shifts for ATP carbon atoms C1´ and C5´ observed in the presence of Na+ or Tris+ suggest alterations in the residues surrounding the bound nucleotide, hydrogen bonding and/or conformation of the ribose ring. This is taken as evidence for a long-distance communication between the Na+-filled ion sites in the membrane interior and the nucleotide binding site in the cytoplasmic domain and reflects the first conformational change ultimately leading to phosphorylation of the enzyme. Stopped-flow fluorescence measurements with the nucleotide analog eosin show that the dissociation rate constant for eosin is larger in Tris+ than in Na+, giving kinetic evidence for the difference in structural effects of Na+ and Tris+. According to the recent crystal structure of the E1•AlF4 -•ADP•3Na+-form the coupling between the ion binding sites and the nucleotide side is mediated by - among others - the M5-helix.

U2 - 10.1021/acs.biochem.5b00893

DO - 10.1021/acs.biochem.5b00893

M3 - Journal article

VL - 54

SP - 7041

EP - 7047

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 47

ER -