Comparing crystal structures of Ca2+-ATPase in the presence of different lipids

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Comparing crystal structures of Ca2+-ATPase in the presence of different lipids. / Drachmann, Nikolaj D; Olesen, Claus; Møller, Jesper V; Guo, Zheng; Bublitz, Maike; Nissen, Poul.

I: F E B S Journal, Bind 281, Nr. 18, 09.2014, s. 4249-4262.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

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Drachmann, Nikolaj D ; Olesen, Claus ; Møller, Jesper V ; Guo, Zheng ; Bublitz, Maike ; Nissen, Poul. / Comparing crystal structures of Ca2+-ATPase in the presence of different lipids. I: F E B S Journal. 2014 ; Bind 281, Nr. 18. s. 4249-4262.

Bibtex

@article{af7282f2c1ac41a993fb79ece8801f6c,
title = "Comparing crystal structures of Ca2+-ATPase in the presence of different lipids",
abstract = "The activity of the sarco/endoplasmic reticulum Ca(2+) -ATPase (SERCA) depends strongly on the lipid composition of the surrounding membrane. Yet, structural information on SERCA-lipid interaction is still relatively scarce, and the influence of different lipids on the enzyme is not well understood. We have analyzed SERCA crystal structures in the presence of four different phosphatidylcholine lipids of different lengths and double-bond compositions, and we find three different binding sites for lipid head groups, which are apparently independent of the acyl moiety of the lipids used. By comparison with other available SERCA structures with bound lipids, we find a total of five recurring sites, two of which are specific to certain conformational states of the enzyme, two others are state-independent, and one is a crucial site for crystal formation. Three of the binding sites overlap with or are in close vicinity to known binding sites for various SERCA-specific inhibitors and regulators, e.g. thapsigargin, sarcolipin/phospholamban and cyclopiazonic acid. Whereas the transient sites are amenable to a transient, regulatory influence of lipid molecules, the state-independent sites probably provide a flexible anchoring of the protein in the fluid bilayer.",
author = "Drachmann, {Nikolaj D} and Claus Olesen and M{\o}ller, {Jesper V} and Zheng Guo and Maike Bublitz and Poul Nissen",
note = "{\textcopyright} 2014 FEBS.",
year = "2014",
month = sep,
doi = "10.1111/febs.12957",
language = "English",
volume = "281",
pages = "4249--4262",
journal = "F E B S Journal",
issn = "1742-464X",
publisher = "Wiley-Blackwell Publishing Ltd.",
number = "18",

}

RIS

TY - JOUR

T1 - Comparing crystal structures of Ca2+-ATPase in the presence of different lipids

AU - Drachmann, Nikolaj D

AU - Olesen, Claus

AU - Møller, Jesper V

AU - Guo, Zheng

AU - Bublitz, Maike

AU - Nissen, Poul

N1 - © 2014 FEBS.

PY - 2014/9

Y1 - 2014/9

N2 - The activity of the sarco/endoplasmic reticulum Ca(2+) -ATPase (SERCA) depends strongly on the lipid composition of the surrounding membrane. Yet, structural information on SERCA-lipid interaction is still relatively scarce, and the influence of different lipids on the enzyme is not well understood. We have analyzed SERCA crystal structures in the presence of four different phosphatidylcholine lipids of different lengths and double-bond compositions, and we find three different binding sites for lipid head groups, which are apparently independent of the acyl moiety of the lipids used. By comparison with other available SERCA structures with bound lipids, we find a total of five recurring sites, two of which are specific to certain conformational states of the enzyme, two others are state-independent, and one is a crucial site for crystal formation. Three of the binding sites overlap with or are in close vicinity to known binding sites for various SERCA-specific inhibitors and regulators, e.g. thapsigargin, sarcolipin/phospholamban and cyclopiazonic acid. Whereas the transient sites are amenable to a transient, regulatory influence of lipid molecules, the state-independent sites probably provide a flexible anchoring of the protein in the fluid bilayer.

AB - The activity of the sarco/endoplasmic reticulum Ca(2+) -ATPase (SERCA) depends strongly on the lipid composition of the surrounding membrane. Yet, structural information on SERCA-lipid interaction is still relatively scarce, and the influence of different lipids on the enzyme is not well understood. We have analyzed SERCA crystal structures in the presence of four different phosphatidylcholine lipids of different lengths and double-bond compositions, and we find three different binding sites for lipid head groups, which are apparently independent of the acyl moiety of the lipids used. By comparison with other available SERCA structures with bound lipids, we find a total of five recurring sites, two of which are specific to certain conformational states of the enzyme, two others are state-independent, and one is a crucial site for crystal formation. Three of the binding sites overlap with or are in close vicinity to known binding sites for various SERCA-specific inhibitors and regulators, e.g. thapsigargin, sarcolipin/phospholamban and cyclopiazonic acid. Whereas the transient sites are amenable to a transient, regulatory influence of lipid molecules, the state-independent sites probably provide a flexible anchoring of the protein in the fluid bilayer.

U2 - 10.1111/febs.12957

DO - 10.1111/febs.12957

M3 - Journal article

C2 - 25103814

VL - 281

SP - 4249

EP - 4262

JO - F E B S Journal

JF - F E B S Journal

SN - 1742-464X

IS - 18

ER -