Mechanisms of TonB-catalyzed iron transport through the enteric bacterial cell envelope.
The recent solution of enteric bacterial porin structure, and new insights into the mechanism by which outer membrane receptor proteins recognize and internalize specific ligands, advocates the re-evaluation of TonB-dependent transport physiology. In this minireview we discuss the potential structural features of siderophore receptors and TonB, and use this analysis to evaluate both existing and new models of energy and signal transduction from the inner membrane to the outer membrane of gram-negative bacteria.
Klebba
P E
PE
Department of Microbiology, Medical College of Wisconsin, Milwaukee 53226.
Rutz
J M
JM
Liu
J
J
Murphy
C K
CK
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism*; D004755:Enterobacteriaceae / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins; D007501:Iron / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D008961:Models, Structural; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; C057616:tonB protein, Bacteria; C489181:tonB protein, E coli; D007501:Iron