NMR studies of the fifth transmembrane segment of sarcoplasmic reticulum Ca2+-ATPase reveals a hinge close to the Ca2+-ligating residues

G. Nielsen; A. Malmendal; A. Meissner; J.V. Møller; N.Chr. Nielsen

doi:10.1016/S0014-5793(03)00448-4

NMR studies of the fifth transmembrane segment of sarcoplasmic reticulum Ca2+-ATPase reveals a hinge close to the Ca2+-ligating residues

G. Nielsen, A. Malmendal, A. Meissner, J.V. Møller, N.Chr. Nielsen^*

^*Corresponding author

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

Abstract

Two recent X-ray structures have tremendously increased the understanding of the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA) and related proteins. Both structures show the fifth transmembrane span (M5) as a single continuous $-helix. The inherent structural and dynamic features of this span (Lys758-Glu785) were studied in isolation in sodium dodecyl sulfate (SDS) micelles using liquid-state nuclear magnetic resonance (NMR) spectroscopy. We find that a flexible region (Ile765-Asn768) is interrupting the $-helix. The location of the flexible region near the Ca2+binding residues Asn768 and Glu771 suggests that together with a similar region in M6 it has a hinge function that may be important for cooperative Ca2+binding and occlusion. textcopyright 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

Originalsprog	Engelsk
Tidsskrift	FEBS Letters
Vol/bind	544
Udgave nummer	1-3
Sider (fra-til)	50-56
ISSN	0014-5793
DOI	https://doi.org/10.1016/S0014-5793(03)00448-4
Status	Udgivet - 2003
Udgivet eksternt	Ja

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This article has been found as a ’Free Version’ from the Publisher on June 23 2020. When access to the article closes, please notify [email protected]

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title = "NMR studies of the fifth transmembrane segment of sarcoplasmic reticulum Ca2+-ATPase reveals a hinge close to the Ca2+-ligating residues",

abstract = "Two recent X-ray structures have tremendously increased the understanding of the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA) and related proteins. Both structures show the fifth transmembrane span (M5) as a single continuous $-helix. The inherent structural and dynamic features of this span (Lys758-Glu785) were studied in isolation in sodium dodecyl sulfate (SDS) micelles using liquid-state nuclear magnetic resonance (NMR) spectroscopy. We find that a flexible region (Ile765-Asn768) is interrupting the $-helix. The location of the flexible region near the Ca2+binding residues Asn768 and Glu771 suggests that together with a similar region in M6 it has a hinge function that may be important for cooperative Ca2+binding and occlusion. textcopyright 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.",

keywords = "Ca -ATPase 2+, Fifth transmembrane segment M5, Membrane protein, Micelle, Nuclear magnetic resonance, Sarcoplasmic reticulum, Sodium dodecyl sulfate",

author = "G. Nielsen and A. Malmendal and A. Meissner and J.V. M{\o}ller and N.Chr. Nielsen",

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T1 - NMR studies of the fifth transmembrane segment of sarcoplasmic reticulum Ca2+-ATPase reveals a hinge close to the Ca2+-ligating residues

AU - Nielsen, G.

AU - Malmendal, A.

AU - Meissner, A.

AU - Møller, J.V.

AU - Nielsen, N.Chr.

N1 - This article has been found as a ’Free Version’ from the Publisher on June 23 2020. When access to the article closes, please notify [email protected]

PY - 2003

Y1 - 2003

N2 - Two recent X-ray structures have tremendously increased the understanding of the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA) and related proteins. Both structures show the fifth transmembrane span (M5) as a single continuous $-helix. The inherent structural and dynamic features of this span (Lys758-Glu785) were studied in isolation in sodium dodecyl sulfate (SDS) micelles using liquid-state nuclear magnetic resonance (NMR) spectroscopy. We find that a flexible region (Ile765-Asn768) is interrupting the $-helix. The location of the flexible region near the Ca2+binding residues Asn768 and Glu771 suggests that together with a similar region in M6 it has a hinge function that may be important for cooperative Ca2+binding and occlusion. textcopyright 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

AB - Two recent X-ray structures have tremendously increased the understanding of the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA) and related proteins. Both structures show the fifth transmembrane span (M5) as a single continuous $-helix. The inherent structural and dynamic features of this span (Lys758-Glu785) were studied in isolation in sodium dodecyl sulfate (SDS) micelles using liquid-state nuclear magnetic resonance (NMR) spectroscopy. We find that a flexible region (Ile765-Asn768) is interrupting the $-helix. The location of the flexible region near the Ca2+binding residues Asn768 and Glu771 suggests that together with a similar region in M6 it has a hinge function that may be important for cooperative Ca2+binding and occlusion. textcopyright 2003 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

KW - Ca -ATPase 2+

KW - Fifth transmembrane segment M5

KW - Membrane protein

KW - Micelle

KW - Nuclear magnetic resonance

KW - Sarcoplasmic reticulum

KW - Sodium dodecyl sulfate

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M3 - Journal article

SN - 0014-5793

VL - 544

SP - 50

EP - 56

JO - FEBS Letters

JF - FEBS Letters

IS - 1-3

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