Mutual adaptation of a membrane protein and its lipid bilayer during conformational changes

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Mutual adaptation of a membrane protein and its lipid bilayer during conformational changes. / Sonntag, Yonathan; Musgaard, Maria; Olesen, Claus; Schiøtt, Birgit; Møller, Jesper Vuust; Nissen, Poul; Thøgersen, Lea.

I: Nature Communications, Bind 2, 2011, s. 304.

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

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@article{4ef48bbd05344f03afcddcbcafe75838,
title = "Mutual adaptation of a membrane protein and its lipid bilayer during conformational changes",
abstract = "The structural elucidation of membrane proteins continues to gather pace, but we know little about their molecular interactions with the lipid environment or how they interact with the surrounding bilayer. Here, with the aid of low-resolution X-ray crystallography, we present direct structural information on membrane interfaces as delineated by lipid phosphate groups surrounding the sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA) in its phosphorylated and dephosphorylated Ca(2+)-free forms. The protein-lipid interactions are further analysed using molecular dynamics simulations. We find that SERCA adapts to membranes of different hydrophobic thicknesses by inducing local deformations in the lipid bilayers and by undergoing small rearrangements of the amino-acid side chains and helix tilts. These mutually adaptive interactions allow smooth transitions through large conformational changes associated with the transport cycle of SERCA, a strategy that may be of general nature for many membrane proteins.",
keywords = "Crystallography, X-Ray, Hydrophobic and Hydrophilic Interactions, Lipid Bilayers, Models, Molecular, Molecular Conformation, Molecular Dynamics Simulation, Phosphorylation, Protein Structure, Secondary, Protein Structure, Tertiary, Sarcoplasmic Reticulum Calcium-Transporting ATPases",
author = "Yonathan Sonntag and Maria Musgaard and Claus Olesen and Birgit Schi{\o}tt and M{\o}ller, {Jesper Vuust} and Poul Nissen and Lea Th{\o}gersen",
year = "2011",
doi = "10.1038/ncomms1307",
language = "English",
volume = "2",
pages = "304",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - Mutual adaptation of a membrane protein and its lipid bilayer during conformational changes

AU - Sonntag, Yonathan

AU - Musgaard, Maria

AU - Olesen, Claus

AU - Schiøtt, Birgit

AU - Møller, Jesper Vuust

AU - Nissen, Poul

AU - Thøgersen, Lea

PY - 2011

Y1 - 2011

N2 - The structural elucidation of membrane proteins continues to gather pace, but we know little about their molecular interactions with the lipid environment or how they interact with the surrounding bilayer. Here, with the aid of low-resolution X-ray crystallography, we present direct structural information on membrane interfaces as delineated by lipid phosphate groups surrounding the sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA) in its phosphorylated and dephosphorylated Ca(2+)-free forms. The protein-lipid interactions are further analysed using molecular dynamics simulations. We find that SERCA adapts to membranes of different hydrophobic thicknesses by inducing local deformations in the lipid bilayers and by undergoing small rearrangements of the amino-acid side chains and helix tilts. These mutually adaptive interactions allow smooth transitions through large conformational changes associated with the transport cycle of SERCA, a strategy that may be of general nature for many membrane proteins.

AB - The structural elucidation of membrane proteins continues to gather pace, but we know little about their molecular interactions with the lipid environment or how they interact with the surrounding bilayer. Here, with the aid of low-resolution X-ray crystallography, we present direct structural information on membrane interfaces as delineated by lipid phosphate groups surrounding the sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA) in its phosphorylated and dephosphorylated Ca(2+)-free forms. The protein-lipid interactions are further analysed using molecular dynamics simulations. We find that SERCA adapts to membranes of different hydrophobic thicknesses by inducing local deformations in the lipid bilayers and by undergoing small rearrangements of the amino-acid side chains and helix tilts. These mutually adaptive interactions allow smooth transitions through large conformational changes associated with the transport cycle of SERCA, a strategy that may be of general nature for many membrane proteins.

KW - Crystallography, X-Ray

KW - Hydrophobic and Hydrophilic Interactions

KW - Lipid Bilayers

KW - Models, Molecular

KW - Molecular Conformation

KW - Molecular Dynamics Simulation

KW - Phosphorylation

KW - Protein Structure, Secondary

KW - Protein Structure, Tertiary

KW - Sarcoplasmic Reticulum Calcium-Transporting ATPases

U2 - 10.1038/ncomms1307

DO - 10.1038/ncomms1307

M3 - Journal article

C2 - 21556058

VL - 2

SP - 304

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

ER -