Functional Characterization of the Shigella dysenteriae Heme ABC Transporter
journal contributionposted on 05.08.2008, 00:00 authored by Kimberly A. Burkhard, Angela Wilks
The heme ATP binding cassette (ABC) transporter, ShuUV, of Shigella dysenteriae has been incorporated into proteoliposomes. Functional characterization of ShuUV revealed that ATP hydrolysis and transport of heme from the periplasmic binding protein, ShuT, to the cytoplasmic binding protein, ShuS, are coupled. Site-directed mutagenesis of ShuT residues proposed to be required for stabilization of the complex abolished heme transport. Furthermore, residues His-252 and His-262, located in the translocation channel of ShuU, were required for the release of heme from ShuT and translocation to ShuS. The initial functional characterization of an in vitro heme uptake system provides a platform for future spectroscopic studies.
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heme uptake systemShuSShuUVFunctional CharacterizationShigella dysenteriaeperiplasmic binding proteincytoplasmic binding proteinheme transportShuT residuesfuture spectroscopic studiesShigella dysenteriae Heme ABC TransporterThe heme ATP binding cassetteFunctional characterizationtranslocation channelATP hydrolysis