11 The ABC Transporter Systems

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The ATP-binding cassette (ABC) transporter systems are a conserved superfamily of multisubunit permeases that are found in all living organisms. Bacterial ABC transporters can be either importers or exporters. The ABC proteins form the largest paralogous family of proteins in . It was initially predicted as a daunorubicin exporter on the basis of its similarity to the locus from . Transcriptome analysis of expression in macrophages showed that 454 genes were induced and 147 genes were repressed in activated or resting macrophages at 24 hours compared with broth culture. In several bacteria, peptide transport can be important for nutrition of the cell, signaling processes such as regulation of gene expression, sporulation, chemotaxis, competence, and virulence. Phosphate is another essential anion that is also transported by one or several multisubunits ABC permeases in mycobacteria. The gene has been shown to be required for macrophage survival and also has been identified twice as being essential for survival of in mice. The phosphate transport system (Pst) from is a tightly regulated high-affinity system encoded by three putative operons, suggesting that the bacteria are involved in subtle biochemical adaptations of for their survival under varying conditions during the infectious cycle. Active multidrug efflux pumps and the mycobacterial cell wall permeability barrier are the mechanisms that are thought to be potentially involved in the natural drug resistance of mycobacteria.

Citation: Content J, Peirs P. 2008. 11 The ABC Transporter Systems, p 185-199. In Daffé M, Reyrat J, Avenir G (ed), The Mycobacterial Cell Envelope. ASM Press, Washington, DC. doi: 10.1128/9781555815783.ch11
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Image of Figure 1.
Figure 1.

Ribbon diagram of the vitamin BBtuCDF, ABC permease protein structure. The transporter is assembled from two membrane-spanning BtuC subunits and two ABC cassettes BtuD. At the ATP binding sites, cyclotetravanadate molecules are bound to the transporter (ball-and-stick models at the BtuD interface). Vitamin B is delivered to the periplasmic side of the transporter by a binding protein (BtuF), then translocated through a pathway provided at the interface of the two membrane-spanning BtuC subunits. It finally exits into the cytoplasm at the large gap between the four subunits. This transport cycle is powered by the hydrolysis of ATP by the ABC cassettes BtuD. Reprinted from Locher and Borths ( ), with permission of the authors.

Citation: Content J, Peirs P. 2008. 11 The ABC Transporter Systems, p 185-199. In Daffé M, Reyrat J, Avenir G (ed), The Mycobacterial Cell Envelope. ASM Press, Washington, DC. doi: 10.1128/9781555815783.ch11
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Image of Figure 2.
Figure 2.

Topological organization of the prototypical ABC transporters. ABC transporters are classified as importers and exporters, depending on the direction of translocation of their substrate (indicated by an arrow). The prokaryotic prototype is composed of two membrane-spanning domains (MSDs) and two nucleotide-binding domains (NBDs) expressed as independent polypeptides. SBP indicates the presence of a substrate binding protein, usually present in importers. This figure was adapted from ).

Citation: Content J, Peirs P. 2008. 11 The ABC Transporter Systems, p 185-199. In Daffé M, Reyrat J, Avenir G (ed), The Mycobacterial Cell Envelope. ASM Press, Washington, DC. doi: 10.1128/9781555815783.ch11
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Image of Figure 3.
Figure 3.

Maltose transport in . The maltose-binding protein (MBP) undergoes a conformational change from an open to a closed conformation on binding maltose in the periplasm. The transport complex (FGK) consists of two membrane-spanning subunits (MSD), MalF and MalG, likely consisting of bundles of eight and six α-helices, respectively, and two copies of the cytoplasmic NBD subunit, MalK. In either the open or the closed conformation, MBP binds to nucleotide-free FGK, in which the MalK NBDs are in an open conformation, and the periplasmic entrance to the translocation pathway is closed (P-closed state). MBP in the open conformation can interact with FGK, but only upon binding maltose and closing is it competent to initiate the transport cycle. ATP binding to MalK triggers NBD association, coinciding with simultaneous opening of both MBP and the periplasmic entrance to the translocation pathway (P-open state), allowing the transfer of sugar to FGK. ATP hydrolysis results in disruption of the MalK dimer interface and reorientation of the transmembrane helices to the starting conformation. Modified from Chen et al. ( ), with permission of the publisher.

Citation: Content J, Peirs P. 2008. 11 The ABC Transporter Systems, p 185-199. In Daffé M, Reyrat J, Avenir G (ed), The Mycobacterial Cell Envelope. ASM Press, Washington, DC. doi: 10.1128/9781555815783.ch11
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Table 1.

Reconstituted ABC transporters

Citation: Content J, Peirs P. 2008. 11 The ABC Transporter Systems, p 185-199. In Daffé M, Reyrat J, Avenir G (ed), The Mycobacterial Cell Envelope. ASM Press, Washington, DC. doi: 10.1128/9781555815783.ch11

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