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Binding Protein-dependent Transport Systems

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Publisher Springer
Date 1990 Aug 1
PMID 2229036
Citations 77
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Abstract

Bacterial binding protein-dependent transport systems are the best characterized members of a superfamily of transporters which are structurally, functionally, and evolutionary related to each other. These transporters are not only found in bacteria but also in yeasts, plants, and animals including man, and include both import and export systems. Although any single system is relatively specific, different systems handle very different substrates which can be inorganic ions, amino acids, sugars, large polysaccharides, or even proteins. Some are of considerable medical importance, including Mdr, the protein responsible for multidrug resistance in human tumors, and the product of the cystic fibrosis locus. In this article we review the current state of knowledge on the structure and function of the protein components of these transporters, the mechanism by which transport is mediated, and the role of ATP in the transport process.

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References
1.
Boyd D, Manoil C, Beckwith J . Determinants of membrane protein topology. Proc Natl Acad Sci U S A. 1987; 84(23):8525-9. PMC: 299577. DOI: 10.1073/pnas.84.23.8525. View

2.
Foley M, Brass J, Birmingham J, Cook W, Garland P, Higgins C . Compartmentalization of the periplasm at cell division sites in Escherichia coli as shown by fluorescence photobleaching experiments. Mol Microbiol. 1989; 3(10):1329-36. DOI: 10.1111/j.1365-2958.1989.tb00114.x. View

3.
Quiocho F . Atomic structures of periplasmic binding proteins and the high-affinity active transport systems in bacteria. Philos Trans R Soc Lond B Biol Sci. 1990; 326(1236):341-51; discussion 351-2. DOI: 10.1098/rstb.1990.0016. View

4.
HOBSON A, Weatherwax R, AMES G . ATP-binding sites in the membrane components of histidine permease, a periplasmic transport system. Proc Natl Acad Sci U S A. 1984; 81(23):7333-7. PMC: 392140. DOI: 10.1073/pnas.81.23.7333. View

5.
Hiles I, Higgins C . Peptide uptake by Salmonella typhimurium. The periplasmic oligopeptide-binding protein. Eur J Biochem. 1986; 158(3):561-7. DOI: 10.1111/j.1432-1033.1986.tb09791.x. View