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Article

OMP peptides modulate the activity of DegS protease by differential binding to active and inactive conformations.

Molecular cell - 16 Jan 2009

Sohn Jungsan, Sauer Robert T

Abstract excerpt

Upon sensing misfolded outer-membrane porins (OMPs) in the periplasm, the E. coli DegS protease cleaves RseA, a transmembrane regulator, transmitting a signal to activate cytoplasmic gene expression. Misfolding is detected by binding of normally inaccessible OMP sequences to the DegS-PDZ domain,...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 19150428
DOI: 10.1016/j.molcel.2008.12.017
PMCID: PMC2742306

Genes

OMP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19150428-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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OMP peptides modulate the activity of DegS protease by differential binding to active and inactive conformations.PMID 19150428Read ↗

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