| Literature DB >> 32335504 |
François Thélot1, Benjamin J Orlando2, Yanyan Li3, Maofu Liao4.
Abstract
Gram-negative bacteria possess a dual-membrane envelope, which provides defense against environmental assault, as well as formidable resistance against antibiotics. Lipopolysaccharide (LPS) is the primary lipid component in the outermost membrane leaflet of most Gram-negative bacteria, and plays critical roles in cell envelope formation. Newly synthesized LPS at the cytoplasmic side of the inner membrane is flipped across the inner membrane and pushed across the periplasm by two ATP-binding cassette transporters, MsbA and LptB2FGC, respectively. Both transporters represent promising targets for developing new classes of antibiotics. In this review, we discuss recent advances in understanding the mechanism of LPS translocation driven by MsbA and LptB2FGC, with a particular focus on new findings from structural studies.Entities:
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Year: 2020 PMID: 32335504 PMCID: PMC7442718 DOI: 10.1016/j.sbi.2020.03.005
Source DB: PubMed Journal: Curr Opin Struct Biol ISSN: 0959-440X Impact factor: 6.809