OmpA: a flexible clamp for bacterial cell wall attachment
OmpA: a flexible clamp for bacterial cell wall attachment
The envelope of Gram-negative bacteria is highly complex, containing separate outer and inner membranes and an intervening periplasmic space encompassing a peptidoglycan (PGN) cell wall. The PGN scaffold is anchored non-covalently to the outer membrane via globular OmpA-like domains of various proteins. We report atomically detailed simulations of PGN bound to OmpA in three different states, including the isolated C-terminal domain (CTD), the full-length monomer, or the complete full-length dimeric form. Comparative analysis of dynamics of OmpA CTD from different bacteria helped to identify a conserved PGN-binding mode. The dynamics of full-length OmpA, embedded within a realistic representation of the outer membrane containing full-rough (Ra) lipopolysaccharide, phospholipids, and cardiolipin, suggested how the protein may provide flexible mechanical support to the cell wall. An accurate model of the heterogeneous bacterial cell envelope should facilitate future efforts to develop antibacterial agents.
2227-2236
Samsudin, Mohd
b01e87a0-af50-44d6-bca4-f511c40165f9
Ortiz-Suarez, Maite
ea69c54e-6640-4a6b-9f92-e188d3d243d4
Piggot, Thomas
75829b71-d73b-43d1-b24f-3e70c2c4d0c8
Bond, Peter J.
08f46940-85e8-44c4-a368-d94342a10fd6
Khalid, Syma
90fbd954-7248-4f47-9525-4d6af9636394
6 December 2016
Samsudin, Mohd
b01e87a0-af50-44d6-bca4-f511c40165f9
Ortiz-Suarez, Maite
ea69c54e-6640-4a6b-9f92-e188d3d243d4
Piggot, Thomas
75829b71-d73b-43d1-b24f-3e70c2c4d0c8
Bond, Peter J.
08f46940-85e8-44c4-a368-d94342a10fd6
Khalid, Syma
90fbd954-7248-4f47-9525-4d6af9636394
Samsudin, Mohd, Ortiz-Suarez, Maite, Piggot, Thomas, Bond, Peter J. and Khalid, Syma
(2016)
OmpA: a flexible clamp for bacterial cell wall attachment.
Structure, 24 (12), .
(doi:10.1016/j.str.2016.10.009).
(PMID:27866852)
Abstract
The envelope of Gram-negative bacteria is highly complex, containing separate outer and inner membranes and an intervening periplasmic space encompassing a peptidoglycan (PGN) cell wall. The PGN scaffold is anchored non-covalently to the outer membrane via globular OmpA-like domains of various proteins. We report atomically detailed simulations of PGN bound to OmpA in three different states, including the isolated C-terminal domain (CTD), the full-length monomer, or the complete full-length dimeric form. Comparative analysis of dynamics of OmpA CTD from different bacteria helped to identify a conserved PGN-binding mode. The dynamics of full-length OmpA, embedded within a realistic representation of the outer membrane containing full-rough (Ra) lipopolysaccharide, phospholipids, and cardiolipin, suggested how the protein may provide flexible mechanical support to the cell wall. An accurate model of the heterogeneous bacterial cell envelope should facilitate future efforts to develop antibacterial agents.
Text
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Accepted/In Press date: 16 October 2016
e-pub ahead of print date: 17 November 2016
Published date: 6 December 2016
Organisations:
Faculty of Natural and Environmental Sciences
Identifiers
Local EPrints ID: 405529
URI: http://eprints.soton.ac.uk/id/eprint/405529
ISSN: 0969-2126
PURE UUID: 9e198a30-a4ac-4ff8-81b1-a13a24159ad2
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Date deposited: 07 Feb 2017 11:25
Last modified: 16 Mar 2024 03:56
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Contributors
Author:
Mohd Samsudin
Author:
Maite Ortiz-Suarez
Author:
Thomas Piggot
Author:
Peter J. Bond
Author:
Syma Khalid
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