NMR studies of the fifth transmembrane segment of Na+,K+-ATPase reveals a non-helical ion-binding region

Jarl Underhaug, Louise Odgaard Jakobsen, Mikael Esmann, Anders Malmendal, Niels Chr Nielsen

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

The structure of a synthetic peptide corresponding to the fifth membrane-spanning segment (M5) in Na(+),K(+)-ATPase in sodium dodecyl sulfate (SDS) micelles was determined using liquid-state nuclear magnetic resonance (NMR) spectroscopy. The spectra reveal that this peptide is substantially less alpha-helical than the corresponding M5 peptide of Ca(2+)-ATPase. A well-defined alpha-helix is shown in the C-terminal half of the peptide. Apart from a short helical stretch at the N-terminus, the N-terminal half contains a non-helical region with two proline residues and sequence similarity to a non-structured transmembrane element of the Ca(2+)-ATPase. Furthermore, this region spans the residues implicated in Na(+) and K(+) transport, where they are likely to offer the flexibility needed to coordinate Na(+) as well as K(+) during active transport.

OriginalsprogEngelsk
TidsskriftF E B S Letters
Vol/bind580
Udgave nummer20
Sider (fra-til)4777-83
Antal sider7
ISSN0014-5793
DOI
StatusUdgivet - 4 sep. 2006
Udgivet eksterntJa

Citer dette

Underhaug, Jarl ; Jakobsen, Louise Odgaard ; Esmann, Mikael ; Malmendal, Anders ; Nielsen, Niels Chr. / NMR studies of the fifth transmembrane segment of Na+,K+-ATPase reveals a non-helical ion-binding region. I: F E B S Letters. 2006 ; Bind 580, Nr. 20. s. 4777-83.
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title = "NMR studies of the fifth transmembrane segment of Na+,K+-ATPase reveals a non-helical ion-binding region",
abstract = "The structure of a synthetic peptide corresponding to the fifth membrane-spanning segment (M5) in Na(+),K(+)-ATPase in sodium dodecyl sulfate (SDS) micelles was determined using liquid-state nuclear magnetic resonance (NMR) spectroscopy. The spectra reveal that this peptide is substantially less alpha-helical than the corresponding M5 peptide of Ca(2+)-ATPase. A well-defined alpha-helix is shown in the C-terminal half of the peptide. Apart from a short helical stretch at the N-terminus, the N-terminal half contains a non-helical region with two proline residues and sequence similarity to a non-structured transmembrane element of the Ca(2+)-ATPase. Furthermore, this region spans the residues implicated in Na(+) and K(+) transport, where they are likely to offer the flexibility needed to coordinate Na(+) as well as K(+) during active transport.",
author = "Jarl Underhaug and Jakobsen, {Louise Odgaard} and Mikael Esmann and Anders Malmendal and Nielsen, {Niels Chr}",
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NMR studies of the fifth transmembrane segment of Na+,K+-ATPase reveals a non-helical ion-binding region. / Underhaug, Jarl; Jakobsen, Louise Odgaard; Esmann, Mikael; Malmendal, Anders; Nielsen, Niels Chr.

I: F E B S Letters, Bind 580, Nr. 20, 04.09.2006, s. 4777-83.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - NMR studies of the fifth transmembrane segment of Na+,K+-ATPase reveals a non-helical ion-binding region

AU - Underhaug, Jarl

AU - Jakobsen, Louise Odgaard

AU - Esmann, Mikael

AU - Malmendal, Anders

AU - Nielsen, Niels Chr

PY - 2006/9/4

Y1 - 2006/9/4

N2 - The structure of a synthetic peptide corresponding to the fifth membrane-spanning segment (M5) in Na(+),K(+)-ATPase in sodium dodecyl sulfate (SDS) micelles was determined using liquid-state nuclear magnetic resonance (NMR) spectroscopy. The spectra reveal that this peptide is substantially less alpha-helical than the corresponding M5 peptide of Ca(2+)-ATPase. A well-defined alpha-helix is shown in the C-terminal half of the peptide. Apart from a short helical stretch at the N-terminus, the N-terminal half contains a non-helical region with two proline residues and sequence similarity to a non-structured transmembrane element of the Ca(2+)-ATPase. Furthermore, this region spans the residues implicated in Na(+) and K(+) transport, where they are likely to offer the flexibility needed to coordinate Na(+) as well as K(+) during active transport.

AB - The structure of a synthetic peptide corresponding to the fifth membrane-spanning segment (M5) in Na(+),K(+)-ATPase in sodium dodecyl sulfate (SDS) micelles was determined using liquid-state nuclear magnetic resonance (NMR) spectroscopy. The spectra reveal that this peptide is substantially less alpha-helical than the corresponding M5 peptide of Ca(2+)-ATPase. A well-defined alpha-helix is shown in the C-terminal half of the peptide. Apart from a short helical stretch at the N-terminus, the N-terminal half contains a non-helical region with two proline residues and sequence similarity to a non-structured transmembrane element of the Ca(2+)-ATPase. Furthermore, this region spans the residues implicated in Na(+) and K(+) transport, where they are likely to offer the flexibility needed to coordinate Na(+) as well as K(+) during active transport.

U2 - 10.1016/j.febslet.2006.07.063

DO - 10.1016/j.febslet.2006.07.063

M3 - Journal article

VL - 580

SP - 4777

EP - 4783

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 20

ER -