Braun’s lipoprotein facilitates OmpA interaction with the Escherichia coli cell wall
Braun’s lipoprotein facilitates OmpA interaction with the Escherichia coli cell wall
Gram-negative bacteria such as Escherichia coli are protected by a complex cell envelope. The development of novel therapeutics against these bacteria necessitates a molecular level understanding of the structure-dynamics-function relationships of the various components of the cell envelope. We use atomistic MD simulations to reveal the details of covalent and noncovalent protein interactions that link the outer membrane to the aqueous periplasmic region. We show that the Braun's lipoprotein tilts and bends, and thereby lifts the cell wall closer to the outer membrane. Both monomers and dimers of the outer membrane porin OmpA can interact with peptidoglycan in the presence of Braun's lipoprotein, but in the absence of the latter, only dimers of OmpA show a propensity to form contacts with peptidoglycan. Our study provides a glimpse of how the molecular components of the bacterial cell envelope interact with each other to mediate cell wall attachment in E. coli.
1496-1504
Samsudin, Mohd
b01e87a0-af50-44d6-bca4-f511c40165f9
Boags, Alister
ec8b83d9-0601-4c97-8acc-3a26349a3076
Piggot, Thomas
75829b71-d73b-43d1-b24f-3e70c2c4d0c8
Khalid, Syma
90fbd954-7248-4f47-9525-4d6af9636394
Samsudin, Mohd
b01e87a0-af50-44d6-bca4-f511c40165f9
Boags, Alister
ec8b83d9-0601-4c97-8acc-3a26349a3076
Piggot, Thomas
75829b71-d73b-43d1-b24f-3e70c2c4d0c8
Khalid, Syma
90fbd954-7248-4f47-9525-4d6af9636394
Samsudin, Mohd, Boags, Alister, Piggot, Thomas and Khalid, Syma
(2017)
Braun’s lipoprotein facilitates OmpA interaction with the Escherichia coli cell wall.
Biophysical Journal, 113 (7), .
(doi:10.1016/j.bpj.2017.08.011).
Abstract
Gram-negative bacteria such as Escherichia coli are protected by a complex cell envelope. The development of novel therapeutics against these bacteria necessitates a molecular level understanding of the structure-dynamics-function relationships of the various components of the cell envelope. We use atomistic MD simulations to reveal the details of covalent and noncovalent protein interactions that link the outer membrane to the aqueous periplasmic region. We show that the Braun's lipoprotein tilts and bends, and thereby lifts the cell wall closer to the outer membrane. Both monomers and dimers of the outer membrane porin OmpA can interact with peptidoglycan in the presence of Braun's lipoprotein, but in the absence of the latter, only dimers of OmpA show a propensity to form contacts with peptidoglycan. Our study provides a glimpse of how the molecular components of the bacterial cell envelope interact with each other to mediate cell wall attachment in E. coli.
Text
PG_BLP_BJ_final_with_figures
- Accepted Manuscript
More information
Accepted/In Press date: 2 August 2017
e-pub ahead of print date: 3 October 2017
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Local EPrints ID: 415012
URI: http://eprints.soton.ac.uk/id/eprint/415012
ISSN: 0006-3495
PURE UUID: a2ed8dd2-8c79-4f9b-9afe-9748c86f4000
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Date deposited: 20 Oct 2017 16:31
Last modified: 16 Mar 2024 05:50
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