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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...

Topics

Amino Acid Sequence
Bacterial Outer Membrane Proteins
Bacteriophages
Base Sequence
Cell Membrane
Cloning, Molecular
Endopeptidases
Escherichia coli
Hot Temperature
Molecular Sequence Data
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Conformation

Protein Folding

Receptors, Virus

Source

Identifiers

PMID: 7623380
DOI: 10.1006/jmbi.1995.0403

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7623380-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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