Biochemical analysis of mutations at tyrosine-98 of the S1 subunit of pertussis toxin.

doi:10.1021/bi00172a038

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Article

Biochemical analysis of mutations at tyrosine-98 of the S1 subunit of pertussis toxin.

Biochemistry - 15 Feb 1994

Xu Y, Barbieri J T

Abstract excerpt

Molecular modeling and alignment of the primary amino acid sequence of the S1 subunit (S1) of pertussis toxin (PT) with other members of the family of ADP-ribosylating bacterial exotoxins predicted that tyrosine-98 (Y98) of S1 was a conserved residue among these exotoxins. To extend our understan...

Topics

Adenosine Diphosphate Ribose
Amino Acid Sequence
Conserved Sequence
Escherichia coli
Exotoxins
Gene Expression
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation
Pertussis Toxin
Protein Folding
Subcellular Fractions
Temperature
Transducin
Tyrosine
Virulence Factors, Bordetella

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Identifiers

PMID: 8312278
DOI: 10.1021/bi00172a038

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8312278-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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