TonB-dependent energy transduction between outer and cytoplasmic membranes.
The TonB system of Escherichia coli (and most other Gram-negative bacteria) is distinguished by its importance to iron acquisition, its contribution to bacterial pathogenesis, and a unique and mysterious mechanism of action. This system somehow gathers the potential energy of the cytoplasmic membrane (CM) proton gradient and delivers it to active transporters in the outer membrane (OM). Our understanding of this system is confounded by the challenge of reconciling often contradictory in vivo and in vitro studies that are presented in this review.
Postle
Kathleen
K
Department of Biochemistry and Molecular Biology, The Pennsylvania State University, 301 Althouse Laboratory, University Park, PA 16802, USA. postle@psu.edu
Larsen
Ray A
RA
D000595:Amino Acid Sequence; D001692:Biological Transport / Q000502:physiology; D002462:Cell Membrane / Q000378:metabolism / Q000648:ultrastructure; D004734:Energy Metabolism; D004926:Escherichia coli / Q000166:cytology / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016415:Sequence Alignment
D029968:Escherichia coli Proteins; D008565:Membrane Proteins; C489181:tonB protein, E coli