Evidence from Mutational Analysis for a Single Transmembrane Substrate Binding Site in the Histidine ATP-Binding Cassette Transporter of Salmonella enterica Serovar Typhimurium.

ABSTRACT: The histidine ATP-binding cassette (ABC) transporter of Salmonella enterica serovar Typhimurium is among the best-studied type I ABC import systems. The transporter consists of two transmembrane subunits, HisQ and HisM, and a homodimer of the nucleotide-binding subunit, HisP. Substrates are delivered by two periplasmic solute binding proteins, HisJ and LAO, with preferences for histidine and for lysine, arginine, and ornithine, respectively. A homology model was built by using the arginine-bound crystal structure of the closely related Art(QN)₂ transporter of Thermoanaerobacter tengcongensis as the template. In the homodimeric Art(QN)₂, one substrate molecule is bound to each of the ArtQ subunits, whereas the structural model and sequence alignments pred

SUBMITTER: Heuveling J 

PROVIDER: S-EPMC6304659 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature