Abstract Lipopolysaccharide (LPS) is an essential glycolipid of the outer membrane (OM) of Gram-negative bacteria with a tripartite structure: lipid A, oligosaccharide core and O antigen. Seven essential LPS-transport proteins (LptABCDEFG) move LPS to the cell surface. Lpt proteins are linked by structural homology, featuring a β-jellyroll domain that mediates protein-protein interactions and LPS binding. Analysis of LptA-LPS interaction by fluorescence spectroscopy is used here to evaluate the contribution of each LPS moiety in protein-ligand interactions, comparing the wild-type (wt) protein to the I36D mutant. In addition to a crucial role of lipid A, an unexpected contribution emerges for the core region in recognition and binding of Lpt proteins.

Santambrogio, C., Sperandeo, P., Barbieri, F., Martorana, A., Polissi, A., Grandori, R. (2015). An induced folding process characterizes the partial-loss of function mutant LptAI36D in its interactions with ligands. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 1854(10), 1451-1457 [10.1016/j.bbapap.2015.06.013].

An induced folding process characterizes the partial-loss of function mutant LptAI36D in its interactions with ligands

SANTAMBROGIO, CARLO
Primo
;
SPERANDEO, PAOLA
Secondo
;
MARTORANA, ALESSANDRA MARIA;GRANDORI, RITA
Ultimo
2015

Abstract

Abstract Lipopolysaccharide (LPS) is an essential glycolipid of the outer membrane (OM) of Gram-negative bacteria with a tripartite structure: lipid A, oligosaccharide core and O antigen. Seven essential LPS-transport proteins (LptABCDEFG) move LPS to the cell surface. Lpt proteins are linked by structural homology, featuring a β-jellyroll domain that mediates protein-protein interactions and LPS binding. Analysis of LptA-LPS interaction by fluorescence spectroscopy is used here to evaluate the contribution of each LPS moiety in protein-ligand interactions, comparing the wild-type (wt) protein to the I36D mutant. In addition to a crucial role of lipid A, an unexpected contribution emerges for the core region in recognition and binding of Lpt proteins.
Articolo in rivista - Articolo scientifico
1-Anilino-8-naphthalene sulfonate; Binding site; Circular dichroism; Escherichia coli; Fluorescence spectroscopy; Lipopolysaccharide transport;
1-Anilino-8-naphthalene sulfonate; Binding site; Circular dichroism; Escherichia coli; Fluorescence spectroscopy; Lipopolysaccharide transport; Biochemistry; Biophysics; Analytical Chemistry; Molecular Biology
English
4-ago-2015
2015
1854
10
1451
1457
39625
none
Santambrogio, C., Sperandeo, P., Barbieri, F., Martorana, A., Polissi, A., Grandori, R. (2015). An induced folding process characterizes the partial-loss of function mutant LptAI36D in its interactions with ligands. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 1854(10), 1451-1457 [10.1016/j.bbapap.2015.06.013].
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/95748
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