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Article

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

Biochemistry - 20 Feb 2007

Montagner Caroline, Perier Aurélie, Pichard Sylvain, Vernier Grégory, Ménez André, Gillet Daniel, Forge Vincent, Chenal Alexandre

Abstract excerpt

During intoxication of a cell, the translocation (T) domain of the diphtheria toxin helps the passage of the catalytic domain across the membrane of the endosome into the cytoplasm. We have investigated the behavior of the N-terminal region of the T domain during the successive steps of its interaction with membranes at acidic pH using tryptophan fluorescence, its quenching by brominated lipids, and trypsin...

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Identifiers

PMID: 17249698
DOI: 10.1021/bi602381z

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Behavior of the N-terminal helices of the diphtheria toxin T domain during the successive steps of membrane interaction.PMID 17249698Read ↗

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

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

Structure of the Diphtheria Toxin at Acidic pH: Implications for the Conformational Switching of the Translocation Domain.Semantic proximity Read ↗

The pH-Dependent Trigger in Diphtheria Toxin T Domain Comes with a Safety Latch.Semantic proximity Read ↗

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

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

Membrane translocation assay based on proteolytic cleavage: application to diphtheria toxin T domain.Semantic proximity Read ↗

Acid-triggered membrane insertion of Pseudomonas exotoxin A involves an original mechanism based on pH-regulated tryptophan exposure.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 ↗

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 ↗

Crucial role of H322 in folding of the diphtheria toxin T-domain into the open-channel state.Semantic proximity Read ↗

Constant-pH MD simulations of the protonation-triggered conformational switching in diphtheria toxin translocation domain.Semantic proximity Read ↗

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