Point mutations in transmembrane helices 2 and 3 of ExbB and TolQ affect their activities in Escherichia coli K-12.
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Colicin biologyThe solution structure of the periplasmic domain of the TonB system ExbD protein reveals an unexpected structural homology with siderophore-binding proteinsStructural insight into the role of the Ton complex in energy transductionLegionella pneumophila LbtU acts as a novel, TonB-independent receptor for the legiobactin siderophore.Mapping the interactions between Escherichia coli TolQ transmembrane segments.Mutations in the ExbB cytoplasmic carboxy terminus prevent energy-dependent interaction between the TonB and ExbD periplasmic domainsThe same periplasmic ExbD residues mediate in vivo interactions between ExbD homodimers and ExbD-TonB heterodimers.Mutations in Escherichia coli ExbB transmembrane domains identify scaffolding and signal transduction functions and exclude participation in a proton pathwayCytoplasmic membrane protonmotive force energizes periplasmic interactions between ExbD and TonBEnergetics of colicin import revealed by genetic cross-complementation between the Tol and Ton systems.
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P2860
Point mutations in transmembrane helices 2 and 3 of ExbB and TolQ affect their activities in Escherichia coli K-12.
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name
Point mutations in transmembra ...... ties in Escherichia coli K-12.
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Point mutations in transmembra ...... ties in Escherichia coli K-12.
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prefLabel
Point mutations in transmembra ...... ties in Escherichia coli K-12.
@en
P2860
P1476
Point mutations in transmembra ...... ties in Escherichia coli K-12.
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P2093
Christina Herrmann
Volkmar Braun
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P304
P356
10.1128/JB.186.13.4402-4406.2004
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2004-07-01T00:00:00Z