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Structure of a lipopolysaccharide regulator reveals a road to new antibiotics

Bacteria with two membranes must regulate the production of a surface molecule known as lipopolysaccharide. The structure of an essential signal-transduction protein now reveals how lipopolysaccharide controls its own synthesis.
  1. Russell E. Bishop

    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.

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Feedback inhibition occurs when the product of a metabolic pathway diminishes its own production by triggering a decrease in the activity of a key enzyme in the pathway. Such inhibition controls the production of lipopolysaccharide (LPS) molecules, which are an integral part of the outer membrane of some bacteria. It has long been suspected that the feedback signal responsible for regulating LPS biosynthesis is either LPS itself, or one of its precursors1. But, writing in Nature, Clairfeuille et al.2 add to a flurry of recent work3–5 showing that the membrane protein PbgA is the long-sought LPS signal transducer in the bacterium Escherichia coli. The current study extends our understanding of PbgA by providing a high-resolution structure of the protein bound to LPS.

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Nature 584, 348-349 (2020)

doi: https://doi.org/10.1038/d41586-020-02256-x

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