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Article

Effects of mutations in proline 345 on insertion of diphtheria toxin into model membranes.

The Journal of membrane biology - 15 Jan 1999

Zhan H, Elliott J L, Shen W H, Huynh P D, Finkelstein A, Collier R J

Abstract excerpt

Translocation of the catalytic domain of diphtheria toxin (DT) across the endosomal membrane to the cytoplasm of mammalian cells requires the low-pH-dependent insertion of a hydrophobic helical hairpin (TH8-TH9) that is buried within the T domain of the native protein. Mutations of Pro345, which...

Topics

Animals
Biological Transport
Cell Membrane
Chlorocebus aethiops
Diphtheria Toxin
Liposomes
Mutation
Proline
Vero Cells

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 9916148
DOI: 10.1007/s002329900481

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9916148-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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Effects of mutations in proline 345 on insertion of diphtheria toxin into model membranes.PMID 9916148Read ↗

Role of acidic residues in helices TH8-TH9 in membrane interactions of the diphtheria toxin T domain.Semantic proximity Read ↗

Topography of helices 5-7 in membrane-inserted diphtheria toxin T domain: identification and insertion boundaries of two hydrophobic sequences that do not form a stable transmembrane hairpin.Semantic proximity Read ↗

pH-dependent insertion of proteins into membranes: B-chain mutation of diphtheria toxin that inhibits membrane translocation, Glu-349----Lys.Semantic proximity Read ↗

Behavior of the N-terminal helices of the diphtheria toxin T domain during the successive steps of membrane interaction.Semantic proximity Read ↗

Replacement of C-terminal histidines uncouples membrane insertion and translocation in diphtheria toxin T-domain.Semantic proximity Read ↗

Behavior of the deeply inserted helices in diphtheria toxin T domain: helices 5, 8, and 9 interact strongly and promote pore formation, while helices 6/7 limit pore formation.Semantic proximity Read ↗

Structure-function relationships in diphtheria toxin channels: III. Residues which affect the cis pH dependence of channel conductance.Semantic proximity Read ↗

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Structure and interaction with model membranes of a CNBR peptide of diphtheria toxin B fragment.Semantic proximity Read ↗

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