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Outer membrane proteins OmpA, FhuA, OmpF, EstA, BtuB, and OmpX have unique lipopolysaccharide fingerprints

Outer membrane proteins OmpA, FhuA, OmpF, EstA, BtuB, and OmpX have unique lipopolysaccharide fingerprints
Outer membrane proteins OmpA, FhuA, OmpF, EstA, BtuB, and OmpX have unique lipopolysaccharide fingerprints

The outer membrane of Gram-negative bacteria has a highly complex asymmetrical architecture, containing a mixture of phospholipids in the inner leaflet and almost exclusively lipopolysaccharide (LPS) molecules in the outer leaflet. In E. coli, the outer membrane contains a wide range of proteins with a β barrel architecture, that vary in size from the smallest having eight strands to larger barrels composed of 22 strands. Here we report coarse-grained molecular dynamics simulations of six proteins from the E. coli outer membrane OmpA, OmpX, BtuB, FhuA, OmpF, and EstA in a range of membrane environments, which are representative of the in vivo conditions for different strains of E. coli. We show that each protein has a unique pattern of interaction with the surrounding membrane, which is influenced by the composition of the protein, the level of LPS in the outer leaflet, and the differing mobilities of the lipids in the two leaflets of the membrane. Overall we present analyses from over 200 μs of simulation for each protein.

1549-9618
2608-2619
Shearer, Jonathan
23e5d5b2-0569-4953-9662-96d59ff0a6ef
Jefferies, Damien
5c5b879d-ea31-4ab7-9d55-ceeecb26a59b
Khalid, Syma
90fbd954-7248-4f47-9525-4d6af9636394
Shearer, Jonathan
23e5d5b2-0569-4953-9662-96d59ff0a6ef
Jefferies, Damien
5c5b879d-ea31-4ab7-9d55-ceeecb26a59b
Khalid, Syma
90fbd954-7248-4f47-9525-4d6af9636394

Shearer, Jonathan, Jefferies, Damien and Khalid, Syma (2019) Outer membrane proteins OmpA, FhuA, OmpF, EstA, BtuB, and OmpX have unique lipopolysaccharide fingerprints. Journal of Chemical Theory and Computation, 15 (4), 2608-2619. (doi:10.1021/acs.jctc.8b01059).

Record type: Article

Abstract

The outer membrane of Gram-negative bacteria has a highly complex asymmetrical architecture, containing a mixture of phospholipids in the inner leaflet and almost exclusively lipopolysaccharide (LPS) molecules in the outer leaflet. In E. coli, the outer membrane contains a wide range of proteins with a β barrel architecture, that vary in size from the smallest having eight strands to larger barrels composed of 22 strands. Here we report coarse-grained molecular dynamics simulations of six proteins from the E. coli outer membrane OmpA, OmpX, BtuB, FhuA, OmpF, and EstA in a range of membrane environments, which are representative of the in vivo conditions for different strains of E. coli. We show that each protein has a unique pattern of interaction with the surrounding membrane, which is influenced by the composition of the protein, the level of LPS in the outer leaflet, and the differing mobilities of the lipids in the two leaflets of the membrane. Overall we present analyses from over 200 μs of simulation for each protein.

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Omps_CG_Structure_Damien_noh - Accepted Manuscript
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Accepted/In Press date: 8 March 2019
e-pub ahead of print date: 8 March 2019
Published date: 9 April 2019

Identifiers

Local EPrints ID: 430516
URI: http://eprints.soton.ac.uk/id/eprint/430516
ISSN: 1549-9618
PURE UUID: efd14f70-4ccc-462f-8973-eec58613caf7
ORCID for Syma Khalid: ORCID iD orcid.org/0000-0002-3694-5044

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Date deposited: 02 May 2019 16:30
Last modified: 07 Oct 2020 06:36

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Contributors

Author: Jonathan Shearer
Author: Damien Jefferies
Author: Syma Khalid ORCID iD

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