ABC Proteins: From Bacteria to Man
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Instructor Ancillary Support Materials. Free Shipping Free global shipping No minimum order. Biochemists, microbiologists, molecular biologists, cell biologists, and geneticists. Powered by. Show all reviews. You are connected as. Connect with:. Yephremov, Y. Cao, R. Jetter, A. Jacquat, J. Plant Cell Bevers, L. Hagedoorn, G. Krijger, and W. Tungsten transport protein A WtpA in Pyrococcus furiosus: the first member of a new class of tungstate and molybdate transporters. Bi, Y. Mann, C. Whitfield, and J. Architecture of a channel-forming O-antigen polysaccharide ABC transporter.
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The Yersinia pestis siderophore, yersiniabactin, and the ZnuABC system both contribute to zinc acquisition and the development of lethal septicaemic plague in mice. Bock, C. Tumulka, K. Reichel, J. Hummer, L. Joseph, F. Bernhard, V. Sci Rep 8: Bordignon, E. Grote, and E. The maltose ATP-binding cassette transporter in the 21st century--towards a structural dynamic perspective on its mode of action.
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Acta Neuropathol Commun 6: Cavazza, C. Martin, E. Laffly, H. Lebrette, M. Cherrier, L. Zeppieri, P. Richaud, M. Histidine of the periplasmic binding protein NikA is essential for nickel uptake in Escherichia coli. Chahine, S. Seabrooke, and M. Effects of genetic knock-down of organic anion transporter genes on secretion of fluorescent organic ions by Malpighian tubules of Drosophila melanogaster. Arch Insect Biochem Physiol Chan, Y. McCormick, and R. A new nos gene downstream from nosDFY is essential for dissimilatory reduction of nitrous oxide by Rhizobium Sinorhizobium meliloti.
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Download flyer. ABC transporters are fascinating molecular machines that use the energy of ATP to catalyze the transport of a tremendous variety of substrates across biological membranes in a vectorial fashion. Here, we will summarize our current knowledge of the domain organization and topology of this class of primary transporters.
All ABC transporters analyzed so far are composed of two nucleotide-binding domains NBD and two transmembrane domains TMD that can be arranged in any possible combination. However, additional transmembrane segments or extended NBDs, raise the possibility that these extensions act as platforms to interact with additional proteins with functional or regulatory consequences. In the light of the recent crystal structures of isolated NBDs in different functional states and the structures of intact ABC transporters, we will also focus on the three-dimensional architecture, domain-domain interactions and putative signaling pathways in these membrane proteins that guarantee efficient substrate recognition and translocation in an ATP-dependent manner.
The majority of ABC proteins encode membrane proteins that utilize the energy of ATP binding and hydrolysis to transport a diverse set of compounds. ABC systems are critical to the cellular physiology of prokaryotes, facilitating the import of nutrients, the extrusion of toxins and for DNA repair. In eukaryotes, ABC proteins function primarily as efflux pumps or as import pumps in intracellular organelles playing important roles in protecting organisms from xenobiotics, antigen presentation, cholesterol and lipid transport.
As ABC transporters extrude an unusually large set of chemically diverse compounds, they impede the treatment of microbial infections and human cancers and are implicated in multidrug resistance MDR. Among prokaryotes, ABC proteins segregate into 29 families belonging to three main classes approximating the functional divisions of the ABC system importers, exporters and "other".
However, the vertebrate ABC proteins do not have the functional or organizational diversity of the prokaryotic proteins. The primary focus of this review is to discuss the evolution and structure-function relationship of microbial and mammalian ABC transporters responsible for MDR and the current status of substrate specificity and mechanistic aspects of mammalian ABC drug transporters. Investigations on ATP binding cassette ABC transporters have not only been an academic pursuit; these membrane transporters are central to many inherited disorders and are associated with multidrug resistance in cancer cells and pathogenic microorganisms.
ABC multidrug transporters are capable of exporting a vast number of structurally unrelated compounds. Quantitative structure-activity relationship QSAR analyses of transported substrates, site-directed mutagenesis and use of thiol-reactive or photo-activatable drug analogues have provided useful information regarding the determinants of drug binding by ABC transporters. Recent studies on MsbA from Escherichia coli indicated that residues important for drug selectivity are located in the membrane domains of the transporter close to the leaflet-leaflet interface of the phospholipid bilayer.
These and other insights in substrate binding, substrate translocation and energy-coupling by ABC extrusion systems will be reviewed. Inhibition of bacterial protein translation is a key point of anti-microbial intervention therapy, with numerous antibiotics functioning as inhibitors of protein synthesis. The macrolide, lincosamide and streptogramin antibiotics MLS antibiotics all cause inhibition of protein synthesis by binding to the 50S ribosomal subunit. Resistance to this class of antibiotics is mediated by many different mechanisms, at least one of which involves an unusual class of ABC proteins.
These antibiotic resistance element ARE type ABC proteins do not include membrane spanning segments within the polypeptide and are not linked in operons to membrane spanning regions. A straightforward transport-based explanation for the function of these ABC proteins in antibiotic resistance is therefore difficult to support. We will illustrate the diversity of these ABC proteins, discuss their clinical relevance, and illustrate three potential modes of action.