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Revisiting the interaction between the chaperone Skp and lipopolysaccharide.

Artikel i vetenskaplig tidskrift
Författare Björn Marcus Burmann
Daniel A Holdbrook
Morgane Callon
Peter J Bond
Sebastian Hiller
Publicerad i Biophysical journal
Volym 108
Nummer/häfte 6
Sidor 1516-26
ISSN 1542-0086
Publiceringsår 2015
Publicerad vid
Sidor 1516-26
Språk en
Länkar dx.doi.org/10.1016/j.bpj.2015.01.02...
www.ncbi.nlm.nih.gov/entrez/query.f...
Ämnesord Amino Acid Sequence, Binding Sites, DNA-Binding Proteins, chemistry, genetics, Detergents, chemistry, Dimethylamines, chemistry, Escherichia coli, Escherichia coli Proteins, chemistry, genetics, Lipopolysaccharides, chemistry, Molecular Chaperones, chemistry, genetics, Molecular Dynamics Simulation, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Protein Denaturation, drug effects, Protein Multimerization, drug effects
Ämneskategorier Strukturbiologi

Sammanfattning

The bacterial outer membrane comprises two main classes of components, lipids and membrane proteins. These nonsoluble compounds are conveyed across the aqueous periplasm along specific molecular transport routes: the lipid lipopolysaccharide (LPS) is shuttled by the Lpt system, whereas outer membrane proteins (Omps) are transported by chaperones, including the periplasmic Skp. In this study, we revisit the specificity of the chaperone-lipid interaction of Skp and LPS. High-resolution NMR spectroscopy measurements indicate that LPS interacts with Skp nonspecifically, accompanied by destabilization of the Skp trimer and similar to denaturation by the nonnatural detergent lauryldimethylamine-N-oxide (LDAO). Bioinformatic analysis of amino acid conservation, structural analysis of LPS-binding proteins, and MD simulations further confirm the absence of a specific LPS binding site on Skp, making a biological relevance of the interaction unlikely. Instead, our analysis reveals a highly conserved salt-bridge network, which likely has a role for Skp function.

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