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Article

Sequence changes in the ton box region of BtuB affect its transport activities and interaction with TonB protein.

Journal of bacteriology - 1 Nov 2000

Cadieux N, Bradbeer C, Kadner R J

Abstract excerpt

Uptake of cobalamins by the transporter protein BtuB in the outer membrane of Escherichia coli requires the proton motive force and the transperiplasmic protein TonB. The Ton box sequence near the amino terminus of BtuB is conserved among all TonB-dependent transporters and is the only known site of mutations that confer a transport-defective phenotype which can be suppressed by certain substitutions at residue...

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Identifiers

PMID: 11029413
DOI: 10.1128/JB.182.21.5954-5961.2000
PMCID: PMC94727

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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Sequence changes in the ton box region of BtuB affect its transport activities and interaction with TonB protein.PMID 11029413Read ↗

His(20) provides the sole functionally significant side chain in the essential TonB transmembrane domain.Semantic proximity Read ↗

Monomeric TonB and the Ton box are required for the formation of a high-affinity transporter-TonB complex.Semantic proximity Read ↗

Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions.Semantic proximity Read ↗

Partial suppression of an Escherichia coli TonB transmembrane domain mutation (delta V17) by a missense mutation in ExbB.Semantic proximity Read ↗

Point mutations in two conserved glycine residues within the integral membrane protein FhuB affect iron(III) hydroxamate transport.Semantic proximity Read ↗

Genetic suppression demonstrates interaction of TonB protein with outer membrane transport proteins in Escherichia coli.Semantic proximity Read ↗

Mutations in the ExbB cytoplasmic carboxy terminus prevent energy-dependent interaction between the TonB and ExbD periplasmic domains.Semantic proximity Read ↗

Interdependence of calcium and cobalamin binding by wild-type and mutant BtuB protein in the outer membrane of Escherichia coli.Semantic proximity Read ↗

Multiple extracellular loops contribute to substrate binding and transport by the Escherichia coli cobalamin transporter BtuB.Semantic proximity Read ↗

Energy transduction between membranes. TonB, a cytoplasmic membrane protein, can be chemically cross-linked in vivo to the outer membrane receptor FepA.Semantic proximity Read ↗

BtuB TonB-dependent transporters and BtuG surface lipoproteins form stable complexes for vitamin B12 uptake in gut BacteroidesSemantic proximity Read ↗

Identification of the periplasmic cobalamin-binding protein BtuF of Escherichia coli.Semantic proximity Read ↗

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