An induced folding process characterizes the partial-loss of function mutant LptAI36D in its interactions with ligands
Articolo
Data di Pubblicazione:
2015
Citazione:
An induced folding process characterizes the partial-loss of function mutant LptAI36D in its interactions with ligands / C. Santambrogio, P. Sperandeo, F. Barbieri, A.M. Martorana, A. Polissi, R. Grandori. - In: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS. - ISSN 1570-9639. - 1854:10(2015), pp. 1451-1457. [10.1016/j.bbapap.2015.06.013]
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.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
1-Anilino-8-naphthalene sulfonate; Binding site; Circular dichroism; Escherichia coli; Fluorescence spectroscopy; Lipopolysaccharide transport; Biochemistry; Biophysics; Analytical Chemistry; Molecular Biology
Elenco autori:
C. Santambrogio, P. Sperandeo, F. Barbieri, A.M. Martorana, A. Polissi, R. Grandori
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