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Article

Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme.

Science (New York, N.Y.) - 7 Jan 2005

Xu Min, Arulandu Arockiasamy, Struck Douglas K, Swanson Stephanie, Sacchettini James C, Young Ry

Abstract excerpt

The P1 lysozyme Lyz is secreted to the periplasm of Escherichia coli and accumulates in an inactive membrane-tethered form. Genetic and biochemical experiments show that, when released from the bilayer, Lyz is activated by an intramolecular thiol-disulfide isomerization, which requires a cysteine in its N-terminal SAR (signal-arrest-release) domain. Crystal structures confirm the alternative disulfide linkages in...

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Identifiers

PMID: 15637279
DOI: 10.1126/science.1105143

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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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