tonB Antibody

1. The TonB system embodies a novel means of active transport across the outer membrane for nutrients. PMID: 26283773
2. Avian pathogenic Escherichia coli DeltatonB mutants are safe and protective live-attenuated vaccine candidates. PMID: 25205199
3. This study has demonstrated that TonB is essential for virulence in avian pathogenic Escherichia coli. PMID: 22237011
4. These observations supported the hypothesis that ExbD couples TonB to the protonmotive force, with concomitant transitions of ExbD and TonB periplasmic domains from unenergized to energized heterodimers. PMID: 22100395
5. ExbD-TonB interactions required ExbD transmembrane domain residue D25. PMID: 21984795
6. TonB with asparagine substitution for His20 is fulluy active. PMID: 21665976
7. Taken together, these results indicate that the solved dimeric crystal structures of TonB do not exist in vivo. PMID: 21179522
8. 92-residue C-terminal fragment of TonB from Escherichia coli structure shown by x-ray crystallography PMID: 15522863
9. after input of protonmotive force mediated through ExbB/D and the TonB transmembrane domain, the TonB carboxy-terminus can form a meta-stable high-energy conformation that is not represented by the crystal structure of the carboxy-terminus. PMID: 15612934
10. the TonB box binds to TonB-CTD along the beta3-strand PMID: 15644214
11. Analyses of two recombinant TonB species in complex with FhuA reveals that TonB undergoes a kinetically limiting rearrangement upon initial interaction with FhuA: an intermediate TonB-FhuA complex of 1:1 stoichiometry is detected. PMID: 15736954
12. Results indicate that TonB-CTD binding to the TonB box was interfered by FecA N-terminal domain and a loss of its secondary structure would expose TonB surface area for additional intermolecular interactions. PMID: 16718599
13. In order to obtain additional information on the nature of TonB-dependent outer membrane active transport, we solved the structure of the C-terminal domain of TonB in complex with the cobalamin transporter BtuB PMID: 16741124
14. A complex of BtuB and a fragment ofTonB was formed in the presence of the substrate cyanocobalamin and calcium and was crystallized. PMID: 16820681
15. This study reports a novel mechanism in which TonB acts as a scaffold, directing FhuD to regions within the periplasm where it is poised to accept and deliver siderophore. PMID: 16928679
16. interaction of TonB, an inner membrane protein, with an outer membrane transporter based upon a recent crystal structure of a TonB-transporter complex PMID: 17449669
17. TonB Q160 region may be part of a large disordered region required to span the periplasm and contact an OM transporter. PMID: 17483231
18. the role of the TonB-ExbB-ExbD complex, potentiated by the proton motive force, is to reduce the affinity of the Cbl-binding site, thus increasing the rate of Cbl release into the periplasmic space PMID: 17908684
19. Proton-motive force is required for the interaction of ExbD and TonB periplasmic domains trapped by formaldehyde cross-linking. PMID: 19627500
20. TonB interacts with BtuF, suppporting a model wherein TonB serves as a scaffold to optimally position BtuF for initial binding of cyanocobalamin and for its subsequent release. PMID: 19708689

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KEGG: ecj:JW5195

STRING: 316385.ECDH10B_1367