Touch and go: tying TonB to transport.
The TonB system of Gram-negative bacteria appears to exist for the purpose of transducing the protonmotive force energy from the cytoplasmic membrane, where it is generated, to the outer membrane, where it is needed for active transport of iron siderophores, vitamin B12 and, in pathogens, iron from host-binding proteins. In this review, we bring the reader up to date on the developments in the field since the authors each wrote reviews in this journal in 1990.
Postle
Kathleen
K
School of Molecular Biosciences, Washington State University, Pullman, WA 99164-4234, USA.
Kadner
Robert J
RJ
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism*; D004735:Energy Transfer / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000378:metabolism; D006090:Gram-Negative Bacteria / Q000378:metabolism*; D007501:Iron / Q000378:metabolism; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D011487:Protein Conformation
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C052874:ExbB protein, E coli; D046911:Macromolecular Substances; D008565:Membrane Proteins; C057616:tonB protein, Bacteria; C489181:tonB protein, E coli; D007501:Iron