PMID:28978443

Citation	Samsudin, F, Boags, A, Piggot, TJ and Khalid, S (2017) Braun's Lipoprotein Facilitates OmpA Interaction with the Escherichia coli Cell Wall. Biophys. J. 113:1496-1504
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.
Links	PubMed PMC5627309 Online version:10.1016/j.bpj.2017.08.011
Keywords	Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/metabolism; Cell Adhesion; Cell Wall/metabolism; Escherichia coli/metabolism; Lipoproteins/chemistry; Lipoproteins/metabolism; Molecular Dynamics Simulation; Peptidoglycan/chemistry; Peptidoglycan/metabolism; Protein Multimerization; Structure-Activity Relationship
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