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Article

Roles of the hydrophobic cavity and lid of LolA in the lipoprotein transfer reaction in Escherichia coli.

The Journal of biological chemistry - 10 Feb 2006

Watanabe Shoji, Matsuyama Shin-ichi, Tokuda Hajime

Abstract excerpt

LolA, a periplasmic chaperone, binds to outer membrane-specific lipoproteins released from the inner membrane through the action of an ATP-binding cassette transporter, LolCDE and then transfers them to the outer membrane receptor LolB, thereby mediating the inner to outer membrane transport of lipoproteins. The crystal structure of free LolA revealed that it has an internal hydrophobic cavity, which is...

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Identifiers

PMID: 16354671
DOI: 10.1074/jbc.M509596200

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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.

Related research

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Roles of the hydrophobic cavity and lid of LolA in the lipoprotein transfer reaction in Escherichia coli.PMID 16354671Read ↗

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

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

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

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

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

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

Mechanism of LolCDE as a molecular extruder of bacterial triacylated 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 ↗

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