Journal of Molecular Biology
TonB protein of Salmonella typhimurium: A model for signal transduction between membranes
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Cited by (106)
Iron acquisition pathways and colonization of the inflamed intestine by Salmonella enterica serovar Typhimurium
2016, International Journal of Medical MicrobiologyCitation Excerpt :Iron acquisition through salmochelin is mediated by the iroBCDE and iroN genes, which are responsible for the biosynthesis (iroB), export (iroC), and absorption (iroN) of salmochelin (Hantke et al., 2003; Bäumler et al., 1996). The process of internalization of this siderophore is an energy dependent process, which requires the TonB/ExbB/ExbD protein-complex located at the inner membrane (Hannavy et al., 1990). TonB energizes transport of ferric iron (Fe3+)-siderophore complexes into the periplasm of Gram-negative bacteria by interacting with specific outer membrane transporters (reviewed by Braun and Hantke, 2011), such as IroN.
Elucidating the origin of the ExbBD components of the TonB system through Bayesian inference and maximum-likelihood phylogenies
2013, Molecular Phylogenetics and EvolutionCitation Excerpt :As a result of a number of experimental studies, the overall topologies and functions of the three TonB proteins have been elucidated. Three transmembrane (TM) domains are present in ExbB (Kampfenkel and Braun, 1993), while ExbD and TonB each have one TM domain (Hannavy et al., 1990; Kampfenkel and Braun, 1992; Ollis et al., 2009; Roof et al., 1991). ExbB and ExbD play key roles in transducing the PMF to TonB (Ollis et al., 2009), which undergoes conformational changes, transmitting potential energy to transporters in the outer membrane (Ghosh and Postle, 2005).
ExbD mutants define initial stages in TonB energization
2012, Journal of Molecular BiologyCitation Excerpt :Ligands are still able to bind their respective OM transporters in protonophore-treated cells.14,15 ExbD (141 amino acids) and TonB (239 amino acids) have identical membrane topologies of a single transmembrane domain (TMD), with the majority of each protein occupying the periplasmic space.16–18 ExbB (244 amino acids) has three TMDs, with the majority of its soluble domains localized to the cytoplasm.19,20
TonB/TolA Amino-Terminal Domain Modeling
2007, Methods in EnzymologyCitation Excerpt :Originally predicted to contain a single transmembrane domain (residues 12–32) on the basis of hydrophobicity (Postle and Good, 1983), this region was subsequently shown to mediate the Sec‐dependent partitioning of TonB to the CM (Postle and Skare, 1988). Topological analyses indicate the bulk of TonB localizes to the periplasmic space, confirming a single amino‐terminal anchorage in the CM (Hannavy et al., 1990; Roof et al., 1991). Essential for function (Jaskula et al., 1994; Karlsson et al., 1993), specific interactions between this signal anchor domain and the energy‐harvesting ExbB/ExbD complex provide for the conversion of TonB to the energized state (Larsen et al., 1999).
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
2005, Journal of Biological ChemistryCitation Excerpt :TonB transduces the energy that is needed for active transport of siderophores and vitamin B12 through its cognate outer membrane receptors. The low copy number of TonB molecules compared with the number of TonB-dependent receptors (1) suggests that TonB probes many receptors and transduces energy only to ligand-loaded ones. Transport is initiated by binding of the ligand to the receptor binding site with submicromolar affinity.
TonB-Dependent Transport Across the Bacterial Outer Membrane
2023, Annual Review of Microbiology
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On sabbatical leave from Lawrence University, Appleton, WI 54912, U.S.A.