Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

The Journal of biological chemistry - 12 Sept 2008

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

Abstract excerpt

LolA plays a critical role in the outer membrane sorting of Escherichia coli lipoproteins because it carries a hydrophobic lipoprotein from the inner membrane through the hydrophilic periplasm to the outer membrane receptor LolB. LolA has an incomplete beta-barrel structure composed of 11 beta-strands with an alpha-helical lid forming a hydrophobic cavity inside. The accompanying study revealed that the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cross-Linking Reagents
Share to Cysteine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Disulfides

Share to Lipoproteins

Share to Models, Chemical

Share to Oxidation-Reduction

Share to Periplasmic Binding Proteins

Share to Protein Structure, Secondary

Source

Identifiers

PMID: 18621730
DOI: 10.1074/jbc.M804737200

Provenance

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

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Introduction of a lethal redox switch that controls the opening and closing of the hydrophobic cavity in LolA.PMID 18621730Read ↗

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

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

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

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 ↗

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

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

Suppressors of lapC Mutation Identify New Regulators of LpxC, Which Mediates the First Committed Step in Lipopolysaccharide Biosynthesis.Semantic proximity Read ↗

A mutation in the membrane subunit of an ABC transporter LolCDE complex causing outer membrane localization of lipoproteins against their inner membrane-specific signals.Semantic proximity Read ↗

Borrelia burgdorferi lipoproteins are secreted to the outer surface by default.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.