The University of Southampton
University of Southampton Institutional Repository

Binding From both sides: TolR and full-length OmpA bind and maintain the local structure of the E. coli cell wall

Binding From both sides: TolR and full-length OmpA bind and maintain the local structure of the E. coli cell wall
Binding From both sides: TolR and full-length OmpA bind and maintain the local structure of the E. coli cell wall
We present a molecular modeling and simulation study of the E. coli cell envelope, with a particular focus on the role of TolR, a native protein of the E. coli inner membrane in interactions with the cell wall. TolR has been proposed to bind to peptidoglycan, but the only structure of this protein thus far is in a conformation in which the putative peptidoglycan binding domain is not accessible. We show that a model of the extended conformation of the protein in which this domain is exposed, binds peptidoglycan largely through electrostatic interactions. Non-covalent interactions of TolR and OmpA with the cell wall, from the inner membrane and outer membrane sides respectively, maintain the position of the cell wall even in the absence of Braun’s lipoprotein. The charged residues that mediate the cell-wall interactions of TolR in our simulations, are conserved across a number of species of Gram-negative bacteria.
0969-2126
713-724.e2
Boags, Alister
ec8b83d9-0601-4c97-8acc-3a26349a3076
Samsudin, Firdaus
b01e87a0-af50-44d6-bca4-f511c40165f9
Khalid, Syma
90fbd954-7248-4f47-9525-4d6af9636394
Boags, Alister
ec8b83d9-0601-4c97-8acc-3a26349a3076
Samsudin, Firdaus
b01e87a0-af50-44d6-bca4-f511c40165f9
Khalid, Syma
90fbd954-7248-4f47-9525-4d6af9636394

Boags, Alister, Samsudin, Firdaus and Khalid, Syma (2019) Binding From both sides: TolR and full-length OmpA bind and maintain the local structure of the E. coli cell wall. Structure, 27 (4), 713-724.e2. (doi:10.1016/j.str.2019.01.001).

Record type: Article

Abstract

We present a molecular modeling and simulation study of the E. coli cell envelope, with a particular focus on the role of TolR, a native protein of the E. coli inner membrane in interactions with the cell wall. TolR has been proposed to bind to peptidoglycan, but the only structure of this protein thus far is in a conformation in which the putative peptidoglycan binding domain is not accessible. We show that a model of the extended conformation of the protein in which this domain is exposed, binds peptidoglycan largely through electrostatic interactions. Non-covalent interactions of TolR and OmpA with the cell wall, from the inner membrane and outer membrane sides respectively, maintain the position of the cell wall even in the absence of Braun’s lipoprotein. The charged residues that mediate the cell-wall interactions of TolR in our simulations, are conserved across a number of species of Gram-negative bacteria.

Text
TolR_BLP_OmpA_final - Accepted Manuscript
Restricted to Repository staff only until 31 January 2020.
Request a copy
Text
TolR-BLP_OmpA_suppinfo_final
Restricted to Repository staff only until 26 November 2019.
Request a copy

More information

Accepted/In Press date: 31 December 2018
e-pub ahead of print date: 31 January 2019
Published date: 2 April 2019

Identifiers

Local EPrints ID: 427074
URI: https://eprints.soton.ac.uk/id/eprint/427074
ISSN: 0969-2126
PURE UUID: d8c69b90-7dc9-42c4-8562-eec35a6be688
ORCID for Firdaus Samsudin: ORCID iD orcid.org/0000-0003-2766-4459
ORCID for Syma Khalid: ORCID iD orcid.org/0000-0002-3694-5044

Catalogue record

Date deposited: 21 Dec 2018 16:30
Last modified: 15 Aug 2019 00:41

Export record

Altmetrics

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of https://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×