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Journal of Bacteriology, December 2005, p. 8511-8515, Vol. 187, No. 24
0021-9193/05/$08.00+0 doi:10.1128/JB.187.24.8511-8515.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Department of Microbiology and Immunology, Queen's University, Kingston, Ontario, K7L 3N6, Canada;,1 Laboratoire de Microbiologie et de Génétique, Université Louis-Pasteur, CNRS FRE 2326, Strasbourg, France,2 Department of Biochemistry, Queen's University, Kingston, Ontario, K7L 3N6, Canada3
Received 27 July 2005/ Accepted 19 September 2005
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.
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