Minimal nanodisc without exogenous lipids for stabilizing membrane proteins in detergent-free buffer.


Journal

Biochimica et biophysica acta. Biomembranes
ISSN: 1879-2642
Titre abrégé: Biochim Biophys Acta Biomembr
Pays: Netherlands
ID NLM: 101731713

Informations de publication

Date de publication:
01 04 2019
Historique:
received: 21 09 2018
revised: 17 12 2018
accepted: 24 01 2019
pubmed: 2 2 2019
medline: 27 11 2019
entrez: 2 2 2019
Statut: ppublish

Résumé

Membrane protein stabilization after detergent solubilization presents drawbacks for structural and biophysical studies, in particular that of a reduced stability in detergent micelles. Therefore, alternative methods are required for efficient stabilization. Lipid nanodisc made with the membrane scaffold protein MSP is a valuable system but requires a fine optimization of the lipid to protein ratio. We present here the use of the scaffold protein MSP without added lipids as a minimal system to stabilize membrane proteins. We show that this method is applicable to α-helical and β-strands transmembrane proteins. This method allowed cryo-electron microscopy structural study of the bacterial transporter MexB. A protein quantification indicates that MexB is stabilized by two MSP proteins. This simplified and efficient method proposes a new advance in harnessing the MSP potential to stabilize membrane proteins.

Identifiants

pubmed: 30707889
pii: S0005-2736(19)30024-0
doi: 10.1016/j.bbamem.2019.01.013
pii:
doi:

Substances chimiques

Bacterial Outer Membrane Proteins 0
Buffers 0
Membrane Lipids 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

852-860

Informations de copyright

Copyright © 2019 Elsevier B.V. All rights reserved.

Auteurs

Dimitri Salvador (D)

Univ. Bordeaux, CBMN UMR 5248, Bordeaux INP, F-33600 Pessac, France; CNRS, CBMN UMR5248, F-33600 Pessac, France.

Marie Glavier (M)

Univ. Bordeaux, CBMN UMR 5248, Bordeaux INP, F-33600 Pessac, France; CNRS, CBMN UMR5248, F-33600 Pessac, France.

Guy Schoehn (G)

Université Grenoble Alpes, CNRS, CEA, Institute for Structural Biology (IBS), 38000, Grenoble, France.

Gilles Phan (G)

Laboratoire de Cristallographie et RMN Biologiques, UMR 8015, CNRS, Université Paris Descartes, Faculté de Pharmacie, 4 Avenue de l'Observatoire, 75006 Paris, France.

Jean-Christophe Taveau (JC)

Univ. Bordeaux, CBMN UMR 5248, Bordeaux INP, F-33600 Pessac, France; CNRS, CBMN UMR5248, F-33600 Pessac, France.

Marion Decossas (M)

Univ. Bordeaux, CBMN UMR 5248, Bordeaux INP, F-33600 Pessac, France; CNRS, CBMN UMR5248, F-33600 Pessac, France.

Sophie Lecomte (S)

Univ. Bordeaux, CBMN UMR 5248, Bordeaux INP, F-33600 Pessac, France; CNRS, CBMN UMR5248, F-33600 Pessac, France.

Sébastien Mongrand (S)

Laboratoire de Biogènese Membranaire, UMR 5200, CNRS, Université de Bordeaux, 71 Avenue Edouard Bourlaux, 33883 Villenave d'Ornon Cedex, France.

Cyril Garnier (C)

Laboratoire de Cristallographie et RMN Biologiques, UMR 8015, CNRS, Université Paris Descartes, Faculté de Pharmacie, 4 Avenue de l'Observatoire, 75006 Paris, France.

Isabelle Broutin (I)

Laboratoire de Cristallographie et RMN Biologiques, UMR 8015, CNRS, Université Paris Descartes, Faculté de Pharmacie, 4 Avenue de l'Observatoire, 75006 Paris, France.

Laetitia Daury (L)

Univ. Bordeaux, CBMN UMR 5248, Bordeaux INP, F-33600 Pessac, France; CNRS, CBMN UMR5248, F-33600 Pessac, France.

Olivier Lambert (O)

Univ. Bordeaux, CBMN UMR 5248, Bordeaux INP, F-33600 Pessac, France; CNRS, CBMN UMR5248, F-33600 Pessac, France. Electronic address: o.lambert@cbmn.u-bordeaux.fr.

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Classifications MeSH