Journal
STRUCTURE
Volume 23, Issue 3, Pages 496-504Publisher
CELL PRESS
DOI: 10.1016/j.str.2015.01.001
Keywords
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Funding
- Wellcome Trust New Investigator Award
- BBSRC [BB/I019855/1]
- China Natural Science Foundation of Guangdong Province [S2013010016539]
- BBSRC [BB/I019855/1, BB/L002558/1, BB/H000267/1] Funding Source: UKRI
- EPSRC [EP/J010421/1, EP/M022609/1] Funding Source: UKRI
- MRC [G1100110] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BEP17032, BB/H000267/1, BBS/B/16011, BB/L002558/1, B19456, BB/I019855/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/M022609/1, EP/J010421/1] Funding Source: researchfish
- Medical Research Council [G1100110] Funding Source: researchfish
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Lipopolysaccharide (LPS) is essential for the vitality of most Gram-negative bacteria and plays an important role in bacterial multidrug resistance. The LptD/E translocon inserts LPS into the outer leaflet, the mechanism of which is poorly understood. Here, we report mutagenesis, functional assays, and molecular dynamics simulations of the LptD/E complex, which suggest two distinct pathways for the insertion of LPS. The N-terminal domain of LptD comprises a hydrophobic slide that injects the acyl tails of LPS directly into the outer membrane through an intramembrane hole, while the core oligosaccharide and O-antigen pass a lumen gate that triggers the unzipping of the lateral opening between strands beta 1C and beta 26C of the barrel of LptD, to finalize LPS insertion. Mutation of the LPS transport related residues or block of the LPS transport pathways results in the deaths of Escherichia coli. These findings are important for the development of novel antibiotics.
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