The outer membrane (OM) of Gram-negative bacteria such as
Most Gram‐negative bacteria assemble lipopolysaccharides (LPS) on their surface to form a permeability barrier against many antimicrobials. LPS is synthesized at the inner membrane and then transported to the outer leaflet of the outer membrane. Although the overall LPS structure is conserved, LPS molecules can differ in composition at the species and strain level. Some bacteria also regulate when to modify phosphates on LPS at the inner membrane in order to become resistant to cationic antimicrobial peptides. The multi‐protein Lpt trans‐envelope machine, which transports LPS from the inner to the outer membrane, must therefore handle a variety of substrates. The most poorly understood step in LPS transport is how the ATP‐binding cassette LptB2FG transporter extracts LPS from the inner membrane. Here, we define residue K34 in LptG as a site within the structural cavity of the
- NSF-PAR ID:
- 10073361
- Publisher / Repository:
- Wiley-Blackwell
- Date Published:
- Journal Name:
- Molecular Microbiology
- Volume:
- 109
- Issue:
- 4
- ISSN:
- 0950-382X
- Page Range / eLocation ID:
- p. 541-554
- Format(s):
- Medium: X
- Sponsoring Org:
- National Science Foundation
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