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Article

Opening and closing of the hydrophobic cavity of LolA coupled to lipoprotein binding and release.

The Journal of biological chemistry - 12 Sept 2008

Oguchi Yuki, Takeda Kazuki, Watanabe Shoji, Yokota Naoko, Miki Kunio, Tokuda Hajime

Abstract excerpt

Outer membrane-specific lipoproteins of Escherichia coli are released from the inner membrane through the action of Lol-CDE, which leads to the formation of a complex between the lipoprotein and LolA, a periplasmic chaperone. LolA then transfers lipoproteins to LolB, a receptor in the outer membrane. The structures of LolA and LolB are very similar, having an incomplete beta-barrel covered with an alpha-helical...

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Identifiers

PMID: 18617521
DOI: 10.1074/jbc.M804736200

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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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Opening and closing of the hydrophobic cavity of LolA coupled to lipoprotein binding and release.PMID 18617521Read ↗

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

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

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

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

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

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

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

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