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Mutagenesis and Molecular Modeling Reveal Three Key Extracellular Loops of the Membrane Receptor HasR That Are Involved in Hemophore HasA Binding ^,

Unité des Membranes Bactériennes, Département de Microbiologie, CNRS URA2172,¹ Unité de Résonance Magnétique Nucléaire des Biomolécules, Département de Biologie Structurale, CNRS URA 2185, Institut Pasteur, 25-28 rue du Dr. Roux, 75724 Paris Cedex 15, France²

Received 14 February 2007/ Accepted 24 April 2007

On the basis of the three-dimensional model of the heme/hemophore TonB-dependent outer membrane receptor HasR, mutants with six-residue deletions in the 11 putative extracellular loops were generated. Although all mutants continued to be active TonB-dependent heme transporters, mutations in three loops abolished hemophore HasA binding both in vivo and in vitro.

Published ahead of print on 4 May 2007.

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