Journal
STRUCTURE
Volume 27, Issue 4, Pages 713-+Publisher
CELL PRESS
DOI: 10.1016/j.str.2019.01.001
Keywords
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Funding
- UK Biotechnology and Biological Sciences Research Council [BB/M029573/1]
- Institute for Life Sciences, University of Southampton
- HECBioSim through Engineering and Physical Sciences Research Council [EP/L000253/1]
- BBSRC [BB/M029573/1] Funding Source: UKRI
- EPSRC [EP/L000253/1, EP/M027260/1, EP/R029407/1] Funding Source: UKRI
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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.
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