Published in

National Academy of Sciences, Proceedings of the National Academy of Sciences, 34(113), 2016

DOI: 10.1073/pnas.1602382113

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Gram-negative trimeric porins have specific LPS binding sites that are essential for porin biogenesis

This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Significance Specific and functional interactions between membrane lipids and proteins are increasingly evident across biology. The outer membrane (OM) of gram-negative bacteria such as Escherichia coli is a selective barrier formed by complex lipids (lipopolysaccharides; LPSs) and outer-membrane proteins. The high stability and low permeability of the OM are critical to bacterial growth and pathogenesis. Here, using biochemical and structural techniques, we reveal specific LPS binding sites on OM porin proteins that allow them to stabilize, rather than disrupt, the ordered network of LPS molecules. Furthermore, we demonstrate that one such site is essential for porin assembly in the OM.