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Article

Membrane assembly of circularly permuted variants of the E. coli outer membrane protein OmpA.

Journal of molecular biology - 28 Jul 1995

Koebnik R, Krämer L

Abstract excerpt

The two-domain, 325 residue outer membrane protein OmpA is one of the most abundant proteins of Escherichia coli, playing a role in the maintenance of the integrity of the cell surface. The N-terminal domain, consisting of about 170 amino acid residues, is embedded in the membrane, presumably in the form of a beta-barrel consisting of eight amphipathic transmembrane strands. Pairs of these proposed transmembrane...

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Identifiers

PMID: 7623380
DOI: 10.1006/jmbi.1995.0403

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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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