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

doi:10.1016/j.bbapap.2015.06.013

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Article

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

Biochimica et biophysica acta - 1 Oct 2015

Santambrogio Carlo, Sperandeo Paola, Barbieri Francesca, Martorana Alessandra M, Polissi Alessandra, Grandori Rita

Abstract excerpt

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...

Topics

Amino Acid Substitution
Anilino Naphthalenesulfonates
Aspartic Acid
Biological Transport
Carbohydrate Sequence
Carrier Proteins
Escherichia coli K12
Escherichia coli Proteins
Gene Expression
Isoleucine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Ligands

Lipopolysaccharides

Molecular Sequence Data

Mutation

Protein Binding

Protein Folding

Recombinant Fusion Proteins

Spectrometry, Fluorescence

Source

Open in PubMed

Identifiers

PMID: 26123264
DOI: 10.1016/j.bbapap.2015.06.013

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-26123264-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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