Journal
BIOPHYSICAL JOURNAL
Volume 113, Issue 7, Pages 1496-1504Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2017.08.011
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Funding
- UK Biotechnology and Biological Sciences Research Council [BB/M029573/1]
- NAMRIP, University of Southampton
- Biotechnology and Biological Sciences Research Council [BB/M029573/1, BB/H000658/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/M027260/1] Funding Source: researchfish
- BBSRC [BB/M029573/1, BB/H000658/1] Funding Source: UKRI
- EPSRC [EP/M027260/1] Funding Source: UKRI
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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.
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