Unknown

Dataset Information

0

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

altmetric image

Publications

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]

Similar Datasets

| S-EPMC6981324 | biostudies-literature
| S-EPMC2150924 | biostudies-literature
| S-EPMC4486319 | biostudies-literature
| S-EPMC8672344 | biostudies-literature
| S-EPMC2699512 | biostudies-literature
| S-EPMC5550100 | biostudies-literature
| S-EPMC2795062 | biostudies-literature
| S-EPMC2373534 | biostudies-other
| S-EPMC2144714 | biostudies-other
| S-EPMC298475 | biostudies-other