| HDX-MS performed on BtuB in E. coli outer membranes delineates the luminal domain's allostery and unfolding upon B12 and TonB binding. | HDX-MS performed on BtuB in E. coli outer membranes delineates the luminal domain's allostery and unfolding upon B12 and TonB binding.
Zmyslowski AM, Baxa MC, Gagnon IA, Sosnick TR., Free PMC Article | 05/21/2022 |
| TonB and FepA display confined mobility within Escherichia coli cell and inner membranes. | Confined Mobility of TonB and FepA in Escherichia coli Membranes.
Lill Y, Jordan LD, Smallwood CR, Newton SM, Lill MA, Klebba PE, Ritchie K., Free PMC Article | 07/8/2017 |
| The authors found numerous specific sites of FepA interaction with TonB on the periplasmic face of the FepA cork in addition to the TonB box. | Going Outside the TonB Box: Identification of Novel FepA-TonB Interactions In Vivo.
Gresock MG, Postle K., Free PMC Article | 07/1/2017 |
| The TonB system embodies a novel means of active transport across the outer membrane for nutrients. | From Homodimer to Heterodimer and Back: Elucidating the TonB Energy Transduction Cycle.
Gresock MG, Kastead KA, Postle K., Free PMC Article | 01/16/2016 |
| ExbB-ExbD-TonB form complex in molar ratios of 4:1:1. | Membrane Protein Complex ExbB4-ExbD1-TonB1 from Escherichia coli Demonstrates Conformational Plasticity.
Sverzhinsky A, Chung JW, Deme JC, Fabre L, Levey KT, Plesa M, Carter DM, Lypaczewski P, Coulton JW., Free PMC Article | 07/25/2015 |
| Avian pathogenic Escherichia coli DeltatonB mutants are safe and protective live-attenuated vaccine candidates. | Avian pathogenic Escherichia coli ΔtonB mutants are safe and protective live-attenuated vaccine candidates.
Holden KM, Browning GF, Noormohammadi AH, Markham P, Marenda MS. | 05/23/2015 |
| This study has demonstrated that TonB is essential for virulence in avian pathogenic Escherichia coli. | TonB is essential for virulence in avian pathogenic Escherichia coli.
Holden KM, Browning GF, Noormohammadi AH, Markham PF, Marenda MS. | 06/16/2012 |
| 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. | ExbD mutants define initial stages in TonB energization.
Ollis AA, Postle K., Free PMC Article | 03/3/2012 |
| ExbD-TonB interactions required ExbD transmembrane domain residue D25. | The same periplasmic ExbD residues mediate in vivo interactions between ExbD homodimers and ExbD-TonB heterodimers.
Ollis AA, Postle K., Free PMC Article | 01/21/2012 |
| ExbB(6) and ExbB(6)ExbD(1) are subcomplexes on which the final complex including TonB is assembled | Oligomeric structure of ExbB and ExbB-ExbD isolated from Escherichia coli as revealed by LILBID mass spectrometry.
Pramanik A, Hauf W, Hoffmann J, Cernescu M, Brutschy B, Braun V. | 12/24/2011 |
| TonB with asparagine substitution for His20 is fulluy active. | Taking the Escherichia coli TonB transmembrane domain "offline"? Nonprotonatable Asn substitutes fully for TonB His20.
Swayne C, Postle K., Free PMC Article | 10/1/2011 |
| Taken together, these results indicate that the solved dimeric crystal structures of TonB do not exist in vivo. | The TonB dimeric crystal structures do not exist in vivo.
Postle K, Kastead KA, Gresock MG, Ghosh J, Swayne CD., Free PMC Article | 08/27/2011 |
| 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. | TonB interacts with BtuF, the Escherichia coli periplasmic binding protein for cyanocobalamin.
James KJ, Hancock MA, Gagnon JN, Coulton JW. | 01/21/2010 |
| Proton-motive force is required for the interaction of ExbD and TonB periplasmic domains trapped by formaldehyde cross-linking. | Cytoplasmic membrane protonmotive force energizes periplasmic interactions between ExbD and TonB.
Ollis AA, Manning M, Held KG, Postle K., Free PMC Article | 01/21/2010 |
| TonB binding promotes conformational changes in outer surface-exposed loops of FhuA. | TonB induces conformational changes in surface-exposed loops of FhuA, outer membrane receptor of Escherichia coli.
James KJ, Hancock MA, Moreau V, Molina F, Coulton JW., Free PMC Article | 01/21/2010 |
| 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 | Observations on the calcium dependence and reversibility of cobalamin transport across the outer membrane of Escherichia coli.
Cadieux N, Barekzi N, Bradbeer C. | 01/21/2010 |
| TonB was required for colicin-induced exposure of the FepA TonB box, suggesting that TonB binds FepA at a different site prior to interaction with the TonB box. | Studies on colicin B translocation: FepA is gated by TonB.
Devanathan S, Postle K. | 01/21/2010 |
| TonB Q160 region may be part of a large disordered region required to span the periplasm and contact an OM transporter. | Deletion and substitution analysis of the Escherichia coli TonB Q160 region.
Vakharia-Rao H, Kastead KA, Savenkova MI, Bulathsinghala CM, Postle K., Free PMC Article | 01/21/2010 |
| interaction of TonB, an inner membrane protein, with an outer membrane transporter based upon a recent crystal structure of a TonB-transporter complex | Mechanics of force propagation in TonB-dependent outer membrane transport.
Gumbart J, Wiener MC, Tajkhorshid E., Free PMC Article | 01/21/2010 |
| 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. | Disulphide trapping of an in vivo energy-dependent conformation of Escherichia coli TonB protein.
Ghosh J, Postle K. | 01/21/2010 |
| Results identify specific molecular contacts between TonB and outer membrane receptors such as FhuA that extend beyond the well-characterized Ton box. | Phage display reveals multiple contact sites between FhuA, an outer membrane receptor of Escherichia coli, and TonB.
Carter DM, Gagnon JN, Damlaj M, Mandava S, Makowski L, Rodi DJ, Pawelek PD, Coulton JW. | 01/21/2010 |
| 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. | Interactions between TonB from Escherichia coli and the periplasmic protein FhuD.
Carter DM, Miousse IR, Gagnon JN, Martinez E, Clements A, Lee J, Hancock MA, Gagnon H, Pawelek PD, Coulton JW. | 01/21/2010 |
| 92-residue C-terminal fragment of TonB from Escherichia coli structure shown by x-ray crystallography | Crystal structure of a 92-residue C-terminal fragment of TonB from Escherichia coli reveals significant conformational changes compared to structures of smaller TonB fragments.
Ködding J, Killig F, Polzer P, Howard SP, Diederichs K, Welte W. | 01/21/2010 |
| the 3.3 angstrom resolution crystal structure of the TonB carboxyl-terminal domain in complex with FhuA | Structure of TonB in complex with FhuA, E. coli outer membrane receptor.
Pawelek PD, Croteau N, Ng-Thow-Hing C, Khursigara CM, Moiseeva N, Allaire M, Coulton JW. | 01/21/2010 |
| 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 | Outer membrane active transport: structure of the BtuB:TonB complex.
Shultis DD, Purdy MD, Banchs CN, Wiener MC. | 01/21/2010 |