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

doi:10.1111/j.1432-1033.1996.00941.x

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Article

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

European journal of biochemistry - 1 Nov 1996

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

Abstract excerpt

theta-Toxin (perfringolysin O), secreted by Clostridium perfringens, shares with other known thiol-activated toxins a conserved undecapeptide, ECTGLAWEWWR, located in the C-terminal region of the protein and containing the unique cysteine of the molecule. Single and double amino acid substitution...

Topics

Animals
Bacterial Toxins
Cholesterol
Circular Dichroism
Erythrocyte Membrane
Hemolysin Proteins
Hemolysis
Mutagenesis, Site-Directed
Mutation
Protein Binding
Recombinant Proteins
Sheep
Spectrophotometry, Ultraviolet
Structure-Activity Relationship
Tryptophan

Source

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Identifiers

PMID: 8944786
DOI: 10.1111/j.1432-1033.1996.00941.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8944786-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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