Escherichia coli possesses a TonB-dependent transport system, which exploits the iron-
binding capacity of citrate and its natural abundance. Here, we describe three structures of …

Transcription of the ferric citrate import system is regulated by ferric citrate binding to the
outer membrane transporter FecA. A signal indicating transporter occupancy is relayed …

Both induction of transcription of the ferric citrate transport genes and transport of ferric
citrate by the Escherichia coli outer membrane receptor FecA require energy derived from …

TonB‐dependent iron transporters reside in the outer membranes of Gram‐negative
bacteria, transporting ferric‐complexes into the periplasm by a mechanism requiring proton …

The siderophore transport activities of the two outer membrane proteins FhuA and FecA of
Escherichia coli require the proton motive force of the cytoplasmic membrane. The energy of …

Ferric citrate induces transcription of the ferric citrate transport genes fecABCDE without
entering the cells of Escherichia coli K‐12. Point mutants of the outer membrane‐receptor …

Citrate-mediated iron transport across the cytoplasmic membrane is catalyzed by an ABC
transporter that consists of the periplasmic binding protein FecB, the transmembrane …

TonB-dependent iron transporters present in the outer membranes of Gram-negative
bacteria transport ferric-siderophore complexes into the periplasm. This requires proton …

Siderophore-mediated acquisition systems facilitate iron uptake. We present the
crystallographic structure of the integral outer membrane receptor FecA from Escherichia …

When a strain (arcB-) of Escherichia coli, unable to synthesize the iron transport compound
enterochelin, was transduced to tonB-, it became resistant to phage phi80 and …