Ferric hydroxamate binding protein FhuD from Escherichia coli: mutants in conserved and non-conserved regions

Uptake of iron complexes into the gram-negative bacterial cell requires highly specific outer membrane receptors and specific ATP-dependent (ATP-Binding-Cassette (ABC)) transport systems located in the inner membrane. The latter type of import system is characterized by a periplasmic binding protein...

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Veröffentlicht in:	Biometals 2002-06, Vol.15 (2), p.121-131
Hauptverfasser:	Clarke, Teresa E, Rohrbach, Martin R, Tari, Leslie W, Vogel, Hans J, Köster, Wolfgang
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino acids ATP Bacteria Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism Conserved Sequence - genetics E coli Escherichia coli Escherichia coli - genetics Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Evolution, Molecular Ferric Compounds - metabolism Gram-positive bacteria Hydroxamic Acids - metabolism Membrane Transport Proteins - chemistry Membrane Transport Proteins - genetics Membrane Transport Proteins - metabolism Membranes Models, Molecular Molecular Sequence Data Mutation Periplasmic Binding Proteins - chemistry Periplasmic Binding Proteins - genetics Periplasmic Binding Proteins - metabolism Phenotype Phylogeny Proteins Residues
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