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Abstract
Transport of lipopolysaccharides (LPS) to the surface of the outer membrane is essential for viability of Gram-negative bacteria. Periplasmic LptC and LptA proteins of the LPS transport system (Lpt) are responsible for LPS transfer between the Lpt inner and outer membrane complexes. Here, using a monomeric E. coli LptA mutant, we first show in vivo that a stable LptA oligomeric form is not strictly essential for bacteria. The LptC-LptA complex was characterized by a combination of SAXS and NMR methods and a low resolution model of the complex was determined. We were then able to observe interaction of LPS with LptC, the monomeric LptA mutant as well as with the LptC-LptA complex. A LptC-LPS complex was built based on NMR data in which the lipid moiety of the LPS is buried at the interface of the two β-jellyrolls of the LptC dimer. The selectivity of LPS for this intermolecular surface and the observation of such cavities at homo- or heteromolecular interfaces in LptC and LptA suggests that intermolecular sites are essential for binding LPS during its transport.
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1 Université Grenoble Alpes, Institut de Biologie Structurale, Grenoble cedex 9, France; CEA, DSV, Institut de Biologie Structurale, Grenoble cedex 9, France; CNRS, Institut de Biologie Structurale, Grenoble cedex 9, France
2 University of Milano, Department of Pharmacological and Biomolecular Sciences, Milano, Italy
3 University of Naples Federico II, Department of Chemical Sciences, Napoli, Italy
