The Escherichia coli Lpt transenvelope protein complex for lipopolysaccharide export is assembled via conserved structurally homologous domains.

@article{Villa2013TheEC,
  title={The Escherichia coli Lpt transenvelope protein complex for lipopolysaccharide export is assembled via conserved structurally homologous domains.},
  author={R. Villa and A. Martorana and Suguru Okuda and L. Gourlay and M. Nardini and P. Sperandeo and G. Deh{\`o} and M. Bolognesi and D. Kahne and A. Polissi},
  journal={Journal of bacteriology},
  year={2013},
  volume={195 5},
  pages={
          1100-8
        }
}
Lipopolysaccharide is a major glycolipid component in the outer leaflet of the outer membrane (OM), a peculiar permeability barrier of Gram-negative bacteria that prevents many toxic compounds from entering the cell. Lipopolysaccharide transport (Lpt) across the periplasmic space and its assembly at the Escherichia coli cell surface are carried out by a transenvelope complex of seven essential Lpt proteins spanning the inner membrane (LptBCFG), the periplasm (LptA), and the OM (LptDE), which… Expand
69 Citations
Characterization of lipopolysaccharide transport protein complex
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