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Article

The Escherichia coli Lpt transenvelope protein complex for lipopolysaccharide export is assembled via conserved structurally homologous domains.

Journal of bacteriology - 1 Mar 2013

Villa Riccardo, Martorana Alessandra M, Okuda Suguru, Gourlay Louise J, Nardini Marco, Sperandeo Paola, Dehò Gianni, Bolognesi Martino, Kahne Daniel, Polissi Alessandra

Abstract excerpt

Lipopolysaccharide is a major glycolipid component in the outer leaflet of the outer membrane (OM), a peculiar permeability barrier of Gram-negative bacteria that prevents many toxic compounds from entering the cell. Lipopolysaccharide transport (Lpt) across the periplasmic space and its assembly at the Escherichia coli cell surface are carried out by a transenvelope complex of seven essential Lpt proteins...

Read the complete abstract on PubMed

Topics

ATP-Binding Cassette Transporters
Bacterial Outer Membrane Proteins
Biological Transport
Carrier Proteins
Escherichia coli

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Escherichia coli Proteins

Lipopolysaccharides

Membrane Proteins

Mutation

Protein Structure, Tertiary

Source

Open in PubMed Open full text

Identifiers

PMID: 23292770
DOI: 10.1128/JB.02057-12
PMCID: PMC3571315

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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