Abstract
Iron is an important element, essential for the growth of almost all living cells. Because of the high insolubility of iron(III) in aerobic conditions, many gram-negative bacteria produce, under iron limitation, small iron-chelating compounds called siderophores, together with new outer-membrane proteins, which function as receptors for the ferrisiderophores. Pseudomonas aeruginosa, an important human opportunistic pathogen, produces at least three known siderophores when grown in iron-deficient conditions: pyochelin, salicylate and pyoverdin. This review focuses on pyoverdin and on the ability of FpvA to bind iron-free and ferric-PaA pyoverdin, in the light of recent information gained from biochemical and biophysical studies and of the recently solved 3D-structures of the related ferrichrome FhuA and enterobactin FepA receptors in Escherichia coli.
MeSH terms
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Amino Acid Sequence
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Bacterial Outer Membrane Proteins / chemistry
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Bacterial Outer Membrane Proteins / metabolism*
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Bacterial Proteins / chemistry
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Bacterial Proteins / metabolism*
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Carrier Proteins / chemistry
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Escherichia coli / chemistry
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Escherichia coli Proteins*
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Iron / pharmacokinetics*
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Membrane Proteins / chemistry
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Membrane Proteins / metabolism*
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Models, Molecular
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Molecular Sequence Data
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Oligopeptides*
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Pigments, Biological / chemistry
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Pigments, Biological / metabolism
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Protein Binding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Pseudomonas aeruginosa / metabolism*
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Receptors, Cell Surface*
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Receptors, Virus / chemistry
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Sequence Homology, Amino Acid
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Spectrophotometry
Substances
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Bacterial Outer Membrane Proteins
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Bacterial Proteins
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Carrier Proteins
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Escherichia coli Proteins
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FhuA protein, E coli
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FpvA protein, Pseudomonas aeruginosa
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Membrane Proteins
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Oligopeptides
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Pigments, Biological
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Receptors, Cell Surface
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Receptors, Virus
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enterobactin receptor
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tonB protein, Bacteria
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tonB protein, E coli
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pyoverdin
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Iron