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Article

Structural studies of the Cpx pathway activator NlpE on the outer membrane of Escherichia coli.

Structure (London, England : 1993) - 1 Aug 2007

Hirano Yu, Hossain Md Motarab, Takeda Kazuki, Tokuda Hajime, Miki Kunio

Abstract excerpt

NlpE, an outer membrane lipoprotein, functions during envelope stress responses in Gram-negative bacteria. In Escherichia coli, adhesion to abiotic surfaces has been reported to activate the Cpx pathway in an NlpE-dependent manner. External copper ions are also thought to activate the Cpx pathway mediated by NlpE. We determined the crystal structure of NlpE from E. coli at 2.6 A resolution. The structure showed...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 17698001
DOI: 10.1016/j.str.2007.06.014

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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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