A β-barrel for oil transport through lipid membranes: Dynamic NMR structures of AlkL.


Journal

Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876

Informations de publication

Date de publication:
01 09 2020
Historique:
pubmed: 21 8 2020
medline: 30 10 2020
entrez: 21 8 2020
Statut: ppublish

Résumé

The protein AlkL is known to increase permeability of the outer membrane of bacteria for hydrophobic molecules, yet the mechanism of transport has not been determined. Differing crystal and NMR structures of homologous proteins resulted in a controversy regarding the degree of structure and the role of long extracellular loops. Here we solve this controversy by determining the de novo NMR structure in near-native lipid bilayers, and by accessing structural dynamics relevant to hydrophobic substrate permeation through molecular-dynamics simulations and by characteristic NMR relaxation parameters. Dynamic lateral exit sites large enough to accommodate substrates such as carvone or octane occur through restructuring of a barrel extension formed by the extracellular loops.

Identifiants

pubmed: 32817429
pii: 2002598117
doi: 10.1073/pnas.2002598117
pmc: PMC7474606
doi:

Substances chimiques

Bacterial Outer Membrane Proteins 0
Bacterial Proteins 0
Lipid Bilayers 0
Membrane Lipids 0
Membrane Proteins 0

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

21014-21021

Informations de copyright

Copyright © 2020 the Author(s). Published by PNAS.

Déclaration de conflit d'intérêts

The authors declare no competing interest.

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Auteurs

Tobias Schubeis (T)

Centre de Résonance Magnétique Nucléaire à Très Hauts Champs de Lyon (FRE 2034-CNRS, Université Claude Bernard Lyon 1, École Normale Supérieure Lyon), Université de Lyon, 69100 Villeurbanne, France.

Tanguy Le Marchand (T)

Centre de Résonance Magnétique Nucléaire à Très Hauts Champs de Lyon (FRE 2034-CNRS, Université Claude Bernard Lyon 1, École Normale Supérieure Lyon), Université de Lyon, 69100 Villeurbanne, France.

Csaba Daday (C)

Biomolecular Dynamics Group, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.

Wojciech Kopec (W)

Biomolecular Dynamics Group, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.

Kumar Tekwani Movellan (K)

Department for NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.

Jan Stanek (J)

Centre de Résonance Magnétique Nucléaire à Très Hauts Champs de Lyon (FRE 2034-CNRS, Université Claude Bernard Lyon 1, École Normale Supérieure Lyon), Université de Lyon, 69100 Villeurbanne, France.

Tom S Schwarzer (TS)

Institute of Biochemical Engineering, Technical University of Munich, 85748 Garching, Germany.

Kathrin Castiglione (K)

Institute of Biochemical Engineering, Technical University of Munich, 85748 Garching, Germany.

Bert L de Groot (BL)

Biomolecular Dynamics Group, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.

Guido Pintacuda (G)

Centre de Résonance Magnétique Nucléaire à Très Hauts Champs de Lyon (FRE 2034-CNRS, Université Claude Bernard Lyon 1, École Normale Supérieure Lyon), Université de Lyon, 69100 Villeurbanne, France; Guido.Pintacuda@ens-lyon.fr land@nmr.mpibpc.mpg.de.

Loren B Andreas (LB)

Centre de Résonance Magnétique Nucléaire à Très Hauts Champs de Lyon (FRE 2034-CNRS, Université Claude Bernard Lyon 1, École Normale Supérieure Lyon), Université de Lyon, 69100 Villeurbanne, France; Guido.Pintacuda@ens-lyon.fr land@nmr.mpibpc.mpg.de.
Department for NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.

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