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Article

Mechanisms underlying energy-independent transfer of lipoproteins from LolA to LolB, which have similar unclosed {beta}-barrel structures.

The Journal of biological chemistry - 14 Oct 2005

Taniguchi Naohiro, Matsuyama Shin-Ichi, Tokuda Hajime

Abstract excerpt

The Lol system, comprising five Lol proteins, transfers lipoproteins from the inner to the outer membrane of Escherichia coli. Periplasmic LolA accepts lipoproteins from LolCDE in the inner membrane and immediately transfers them to LolB, a receptor anchored to the outer membrane. The unclosed beta-barrel structures of LolA and LolB are very similar to each other and form hydrophobic cavities for lipoproteins....

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Source

Identifiers

PMID: 16091355
DOI: 10.1074/jbc.M507388200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Mechanisms underlying energy-independent transfer of lipoproteins from LolA to LolB, which have similar unclosed {beta}-barrel structures.PMID 16091355Read ↗

Roles of the hydrophobic cavity and lid of LolA in the lipoprotein transfer reaction in Escherichia coli.Semantic proximity Read ↗

Mutant of LolA, a lipoprotein-specific molecular chaperone of Escherichia coli, defective in the transfer of lipoproteins to LolB.Semantic proximity Read ↗

Opening and closing of the hydrophobic cavity of LolA coupled to lipoprotein binding and release.Semantic proximity Read ↗

Roles of the protruding loop of factor B essential for the localization of lipoproteins (LolB) in the anchoring of bacterial triacylated proteins to the outer membrane.Semantic proximity Read ↗

Novel mutations of the LolCDE complex causing outer membrane localization of lipoproteins despite their inner membrane-retention signals.Semantic proximity Read ↗

Dominant negative mutant of a lipoprotein-specific molecular chaperone, LolA, tightly associates with LolCDE.Semantic proximity Read ↗

Genetic analysis reveals a robust and hierarchical recruitment of the LolA chaperone to the LolCDE lipoprotein transporterSemantic proximity Read ↗

A novel ligand bound ABC transporter, LolCDE, provides insights into the molecular mechanisms underlying membrane detachment of bacterial lipoproteins.Semantic proximity Read ↗

<i>Borrelia burgdorferi</i> BB0346 is an Essential, Structurally Variant LolA Homolog that is Primarily Required for Homeostatic Localization of Periplasmic LipoproteinsSemantic proximity Read ↗

Structural investigation of the interaction between LolA and LolB using NMR.Semantic proximity Read ↗

Introduction of a lethal redox switch that controls the opening and closing of the hydrophobic cavity in LolA.Semantic proximity Read ↗

Defective lipoprotein sorting induces lolA expression through the Rcs stress response phosphorelay system.Semantic proximity Read ↗

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