1. Mutagenesis and molecular modeling reveal three key extracellular loops of the membrane receptor HasR that are involved in hemophore HasA binding
- Author
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Philippe Delepelaire, Clément Barjon, Karine Wecker, Nadia Izadi-Pruneyre, Membranes bactériennes, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Résonance Magnétique Nucléaire des Biomolécules, and Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS)
- Subjects
Models, Molecular ,MESH: Mutation ,Mutant ,MESH: Protein Structure, Secondary ,MESH: Carrier Proteins ,Plasma protein binding ,Heme ,Biology ,Microbiology ,Protein Structure, Secondary ,03 medical and health sciences ,chemistry.chemical_compound ,MESH: Protein Structure, Tertiary ,Bacterial Proteins ,Cell surface receptor ,Structural Biology ,Extracellular ,MESH: Protein Binding ,Molecular Biology ,MESH: Bacterial Proteins ,030304 developmental biology ,MESH: Mutagenesis ,0303 health sciences ,[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM] ,030306 microbiology ,Mutagenesis ,Membrane Proteins ,3. Good health ,Cell biology ,Protein Structure, Tertiary ,chemistry ,Membrane protein ,MESH: Heme ,Mutation ,MESH: Membrane Proteins ,Bacterial outer membrane ,Carrier Proteins ,MESH: Models, Molecular ,Protein Binding - Abstract
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
- 2007