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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.


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.

SUBMITTER: Barjon C 

PROVIDER: S-EPMC1951882 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature

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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.

Barjon Clément C   Wecker Karine K   Izadi-Pruneyre Nadia N   Delepelaire Philippe P  

Journal of bacteriology 20070504 14


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. ...[more]

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