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Article

An intramolecular disulphide bond reduces the efficacy of a lipoprotein plasma membrane sorting signal.

Molecular microbiology - 1 Aug 2003

Robichon Carine, Bonhivers Mélanie, Pugsley Anthony P

Abstract excerpt

To study lipoprotein sorting in Escherichia coli, we devised a novel screen in which sensitivity or resistance to bacteriophage T5 and colicin M reflects the membrane localization of the bacteriophage T5-encoded lipoprotein Llp, which inactivates the outer membrane (OM) T5 receptor (FhuA). When processed by lipoprotein signal peptidase, Llp has a serine at position +2, immediately after the fatty acylated...

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

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Identifiers

PMID: 12890035
DOI: 10.1046/j.1365-2958.2003.03654.x

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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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An intramolecular disulphide bond reduces the efficacy of a lipoprotein plasma membrane sorting signal.PMID 12890035Read ↗

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