Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter.
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Colicin biologyROSET Model of TonB Action in Gram-Negative Bacterial Iron AcquisitionCrystal structure of the dimeric C-terminal domain of TonB reveals a novel foldCrystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand bindingDimerization of TonB is not essential for its binding to the outer membrane siderophore receptor FhuA of Escherichia coliMolecular characterization of the TonB2 protein from the fish pathogen Vibrio anguillarumDifferential effects of mutations in tonB1 on intrinsic multidrug resistance and iron acquisition in Pseudomonas aeruginosaMolecular basis of bacterial outer membrane permeability revisitedGoing Outside the TonB Box: Identification of Novel FepA-TonB Interactions In Vivo.NagA-dependent uptake of N-acetyl-glucosamine and N-acetyl-chitin oligosaccharides across the outer membrane of Caulobacter crescentus.Studies on colicin B translocation: FepA is gated by TonB.Siderophore transport through Escherichia coli outer membrane receptor FhuA with disulfide-tethered cork and barrel domains.Activities of the Serratia marcescens heme receptor HasR and isolated plug and beta-barrel domains: the beta-barrel forms a heme-specific channelMultiple extracellular loops contribute to substrate binding and transport by the Escherichia coli cobalamin transporter BtuB.Mutant analysis of the Escherichia coli FhuA protein reveals sites of FhuA activity.Diffusion through channel derivatives of the Escherichia coli FhuA transport protein.FepA with globular domain deletions lacks activityFhuA barrel-cork hybrids are active transporters and receptors.Exchangeability of N termini in the ligand-gated porins of Escherichia coli.Identification of discrete domains within gonococcal transferrin-binding protein A that are necessary for ligand binding and iron uptake functionsAllosteric Signaling Is Bidirectional in an Outer-Membrane Transport Protein.Sequence changes in the ton box region of BtuB affect its transport activities and interaction with TonB proteinDifferential substrate-induced signaling through the TonB-dependent transporter BtuB.Competing ligands stabilize alternate conformations of the energy coupling motif of a TonB-dependent outer membrane transporter.Monomeric TonB and the Ton box are required for the formation of a high-affinity transporter-TonB complex.Ligand-induced structural changes in the Escherichia coli ferric citrate transporter reveal modes for regulating protein-protein interactions.The N-terminal domain of a TonB-dependent transporter undergoes a reversible stepwise denaturation.Coupling of calcium and substrate binding through loop alignment in the outer-membrane transporter BtuB.Solutes modify a conformational transition in a membrane transport protein.Crystallization and preliminary X-ray crystallographic analysis of the Escherichia coli outer membrane cobalamin transporter BtuB in complex with the carboxy-terminal domain of TonBSubstrate-dependent unfolding of the energy coupling motif of a membrane transport protein determined by double electron-electron resonance.Molecular basis for substrate-dependent transmembrane signaling in an outer-membrane transporter.Mechanics of force propagation in TonB-dependent outer membrane transportSubstrate-dependent transmembrane signaling in TonB-dependent transporters is not conserved.Observations on the calcium dependence and reversibility of cobalamin transport across the outer membrane of Escherichia coli.Mutational analysis of the TonB1 energy coupler of Pseudomonas aeruginosa.The iron- and temperature-regulated cjrBC genes of Shigella and enteroinvasive Escherichia coli strains code for colicin Js uptake.RcnB is a periplasmic protein essential for maintaining intracellular Ni and Co concentrations in Escherichia coli.Control of the ferric citrate transport system of Escherichia coli: mutations in region 2.1 of the FecI extracytoplasmic-function sigma factor suppress mutations in the FecR transmembrane regulatory protein.Characterization of in vitro interactions between a truncated TonB protein from Escherichia coli and the outer membrane receptors FhuA and FepA.
P2860
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P2860
Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter.
description
1999 nî lūn-bûn
@nan
1999 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Site-directed disulfide bondin ...... embrane cobalamin transporter.
@ast
Site-directed disulfide bondin ...... embrane cobalamin transporter.
@en
type
label
Site-directed disulfide bondin ...... embrane cobalamin transporter.
@ast
Site-directed disulfide bondin ...... embrane cobalamin transporter.
@en
prefLabel
Site-directed disulfide bondin ...... embrane cobalamin transporter.
@ast
Site-directed disulfide bondin ...... embrane cobalamin transporter.
@en
P2860
P356
P1476
Site-directed disulfide bondin ...... embrane cobalamin transporter.
@en
P2093
P2860
P304
10673-10678
P356
10.1073/PNAS.96.19.10673
P407
P577
1999-09-01T00:00:00Z