Mutagenesis and molecular modeling reveal three key extracellular loops of the membrane receptor HasR that are involved in hemophore HasA binding.

Clément Barjon (1) , Karine Wecker (2) , Nadia Izadi-Pruneyre (2) , Philippe Delepelaire (1)

1 Membranes bactériennes
2 Résonance Magnétique Nucléaire des Biomolécules

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.

Domains: Life Sciences [q-bio]; Biochemistry, Molecular Biology; Structural Biology [q-bio.BM]

Clément Barjon, Karine Wecker, Nadia Izadi-Pruneyre, Philippe Delepelaire. Mutagenesis and molecular modeling reveal three key extracellular loops of the membrane receptor HasR that are involved in hemophore HasA binding.. Journal of Bacteriology, 2007, 189 (14), pp.5379-82. ⟨10.1128/JB.00251-07⟩. ⟨pasteur-00366344⟩