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- W1010649856 abstract "This chapter discusses the composition and basic features of periplasmic permeases of gram-negative bacteria emphasizing those aspects of periplasmic transport that relate to their energy-coupling mechanism and structural organization. The mechanism of action of eukaryotic transporters is also presented in the chapter. Periplasmic permeases are composed of a receptor (a periplasmic substrate binding protein) and two to three membrane-bound components. All periplasmic permeases have the same overall composition. The similarity in the composition of these permeases indicates a conserved structural organization and mechanism of action despite the vast variety of substrates transported and a common evolutionary origin. Periplasmic permeases typically concentrate substrates against a very large concentration gradient. ATP binding and hydrolysis result in the conformational changes that are transmitted to the rest of the permease, thereby causing the opening of a pore or the creation of a substrate binding site in the membrane-bound complex. Conformational changes may be necessary as a signal for the receptor to release the substrate, which is deeply buried between its two lobes." @default.
- W1010649856 created "2016-06-24" @default.
- W1010649856 creator A5046685224 @default.
- W1010649856 date "1992-01-01" @default.
- W1010649856 modified "2023-10-13" @default.
- W1010649856 title "Bacterial Periplasmic Permeases as Model Systems for the Superfamily of Traffic ATPases, Including the Multidrug Resistance Protein and the Cystic Fibrosis Transmembrane Conductance Regulator" @default.
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- W1010649856 doi "https://doi.org/10.1016/s0074-7696(08)62672-8" @default.
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