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Article

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

Journal of bacteriology - 1 Apr 2007

Larsen Ray A, Deckert Gail E, Kastead Kyle A, Devanathan Surendranathan, Keller Kimberly L, Postle Kathleen

Abstract excerpt

The cytoplasmic membrane protein TonB couples the protonmotive force of the cytoplasmic membrane to active transport across the outer membrane of Escherichia coli. The uncleaved amino-terminal signal anchor transmembrane domain (TMD; residues 12 to 32) of TonB and the integral cytoplasmic membrane proteins ExbB and ExbD are essential to this process, with important interactions occurring among the several TMDs of...

Topics

Amino Acid Sequence
Amino Acid Substitution
Cell Membrane
Escherichia coli
Escherichia coli Proteins
Genotype
Histidine
Kinetics
Membrane Proteins
Molecular Sequence Data
Phenotype

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Plasmids

Recombinant Proteins

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Identifiers

PMID: 17277053
DOI: 10.1128/JB.01925-06
PMCID: PMC1855822

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Click a neighbor to travelStep 1 · 12 closest

His(20) provides the sole functionally significant side chain in the essential TonB transmembrane domain.PMID 17277053Read ↗

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

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

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

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

Targeted disulfide cross-linking of the MotB protein of Escherichia coli: evidence for two H(+) channels in the stator Complex.Semantic proximity Read ↗

Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli.Semantic proximity Read ↗

Systematic conformation-to-phenotype mapping via limited deep-sequencing of proteinsSemantic proximity Read ↗

Engineered pathways for correct disulfide bond oxidation.Semantic proximity Read ↗

Characterization of the exbBD operon of Escherichia coli and the role of ExbB and ExbD in TonB function and stability.Semantic proximity Read ↗

TonB and the gram-negative dilemma.Semantic proximity Read ↗

TonB system, in vivo assays and characterization.Semantic proximity Read ↗

Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway.Semantic proximity Read ↗

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