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Article

Contribution of tryptophan residues to the structural changes in perfringolysin O during interaction with liposomal membranes.

Journal of biochemistry - 1 Jun 1998

Nakamura M, Sekino-Suzuki N, Mitsui K, Ohno-Iwashita Y

Abstract excerpt

Perfringolysin O (theta-toxin) is a cholesterol-binding and pore-forming toxin that shares with other thiol-activated cytolysins a highly conserved sequence, ECTGLAWEWWR (residues 430-440), near the C-terminus. To understand the membrane-insertion and pore-forming mechanisms of the toxin, we eval...

Topics

Animals
Bacterial Toxins
Hemolysin Proteins
Liposomes
Mutation
Protein Binding
Protein Folding
Protein Structure, Secondary
Tryptophan

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 9604004
DOI: 10.1093/oxfordjournals.jbchem.a022054

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9604004-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Contribution of tryptophan residues to the structural changes in perfringolysin O during interaction with liposomal membranes.PMID 9604004Read ↗

Contribution of individual tryptophan residues to the structure and activity of theta-toxin (perfringolysin O), a cholesterol-binding cytolysin.Semantic proximity Read ↗

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