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Structural biology

Lipopolysaccharide rolls out the barrel

Nature volume 511, pages 37–38 (2014)Cite this article

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Two crystal structures of the LptD–LptE protein complex reveal how the cell-wall component lipopolysaccharide is delivered and inserted into the external leaflet of the bacterial outer membrane. See Article p.52 & Letter p.108

The inner membrane of many bacteria is surrounded by a protective cell wall, which includes an outer membrane adorned with a tightly packed layer of lipopolysaccharide (LPS) molecules. LPS is an elaborate phospholipid that is extensively decorated with sugars, and its presence provides a barrier against harmful agents such as detergents and lipophilic ('greasy') antibiotics. Many of the cellular processes by which LPS is assembled and transported to the outer membrane are essential for survival, and thus are targets for the development of new antibiotics. In two papers published in this issue, Dong et al.1 (page 52) and Qiao et al.2 (page 108) present structural studies that disclose a remarkable molecular mechanism by which LPS arrives at its final destination in the outer membrane.

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Figure 1: Structure of the LptD–LptE protein complex.

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Authors and Affiliations

  1. Russell E. Bishop is in the Department of Biochemistry and Biomedical Sciences, and at the Michael G. DeGroote Institute for Infectious Disease Research, McMaster University, Hamilton, Ontario L8S 4K1, Canada.,

    Russell E. Bishop

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  1. Russell E. Bishop
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Correspondence to Russell E. Bishop.

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Bishop, R. Lipopolysaccharide rolls out the barrel. Nature 511, 37–38 (2014). https://doi.org/10.1038/nature13508

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