TonB-dependent iron acquisition: mechanisms of siderophore-mediated active transport.
Cells growing in aerobic environments have developed intricate strategies to overcome the scarcity of iron, an essential nutrient. In gram-negative bacteria, high-affinity iron acquisition requires outer membrane-localized proteins that bind iron chelates at the cell surface and promote their uptake. Transport of bound chelates across the outer membrane depends upon TonB-ExbB-ExbD, a cytoplasmic membrane-localized complex that transduces energy from the proton motive force to high-affinity receptors in the outer membrane. Upon ligand binding to iron chelate receptors, conformational changes are induced, some of which are detected in the periplasm. These structural alterations signal the ligand-loaded status of the receptor and, therefore, the requirement for TonB-dependent energy transduction. Thus, TonB interacts preferentially and directly with ligand-loaded receptors. Such a mechanism ensures the productive use of cellular energy to drive active transport at the outer membrane.
Moeck
G S
GS
Department of Microbiology and Immunology, McGill University, Montreal, Canada. greg.moeck@biomemb.u-psud.fr
Coulton
J W
JW
D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D001693:Biological Transport, Active; D007501:Iron / Q000378:metabolism*; D008024:Ligands; D008565:Membrane Proteins / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000378:metabolism; D017262:Siderophores / Q000378:metabolism*; D015398:Signal Transduction
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D008024:Ligands; D008565:Membrane Proteins; D011956:Receptors, Cell Surface; D017262:Siderophores; C057616:tonB protein, Bacteria; D007501:Iron