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J. Bacteriol. doi:10.1128/JB.00251-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Mutagenesis and molecular modeling reveal 3 key extracellular loops of the membrane receptor HasR involved in hemophore HasA binding

Unité des Membranes Bactériennes, Département de Microbiologie, CNRS URA2172, 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 France

^* To whom correspondence should be addressed. Email: pdelep{at}pasteur.fr.

	Abstract

On the basis of the 3D model of the heme/hemophore TonB-dependent outer membrane receptor HasR, six-residue deletion mutants in the eleven 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.