FpvA-mediated ferric pyoverdine uptake in Pseudomonas aeruginosa: identification of aromatic residues in FpvA implicated in ferric pyoverdine binding and transport.
A number of aromatic residues were seen to cluster in the upper portion of the three-dimensional structure of the FpvA ferric pyoverdine receptor of Pseudomonas aeruginosa, reminiscent of the aromatic binding pocket for ferrichrome in the FhuA receptor of Escherichia coli. Alanine substitutions in three of these, W362, W391, and F795, markedly compromised ferric pyoverdine binding and transport, consistent with a role of FpvA in ferric pyoverdine recognition.
Shen
Jiang-Sheng
JS
Department of Microbiology and Immunology, Queen's University, Kingston, Ontario K7L 3N6, Canada.
Geoffroy
Valérie
V
Neshat
Shadi
S
Jia
Zongchao
Z
Meldrum
Allison
A
Meyer
Jean-Marie
JM
Poole
Keith
K
D019943:Amino Acid Substitution; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D001692:Biological Transport; D004252:DNA Mutational Analysis; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000502:physiology; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D009842:Oligopeptides / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa / Q000378:metabolism*; D011991:Receptors, Virus / Q000737:chemistry / Q000502:physiology
D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; C050900:FhuA protein, E coli; C082326:FpvA protein, Pseudomonas aeruginosa; D009842:Oligopeptides; D011991:Receptors, Virus; C042453:pyoverdin