The ABC maltose transporter

Autor(en): Ehrmann, M
Ehrle, R
Hofmann, E
Boos, W
Schlosser, A
Stichwörter: ACTIVE-TRANSPORT; BINDING CASSETTE TRANSPORTER; Biochemistry & Molecular Biology; ESCHERICHIA-COLI K-12; GENETIC-ANALYSIS; INNER MEMBRANE-PROTEIN; MALK SUBUNIT; Microbiology; NUCLEOTIDE-SEQUENCE; PROTEIN-DEPENDENT TRANSPORT; SALMONELLA-TYPHIMURIUM; STREPTOMYCES-COELICOLOR A3(2)
Erscheinungsdatum: 1998
Herausgeber: BLACKWELL SCIENCE LTD
Journal: MOLECULAR MICROBIOLOGY
Volumen: 29
Ausgabe: 3
Startseite: 685
Seitenende: 694
Zusammenfassung: 
Bacterial ATP-binding cassette (ABC) transporters and their homologues in eukaryotic cells form one of the largest superfamilies known today. They function as primary pumps that couple substrate translocation across the cytoplasmic membrane to ATP hydrolysis. Although ABC transporters have been studied for more than three decades, the structure of these multicomponent systems is unknown, and the mechanism of transport is not understood. This article reviews one of the most widely studied ABC systems, the maltose transporter of Escherichia coli, A first structural model of the transport channel allows discussion of possible mechanisms of transport. In addition, recent experimental evidence suggests that regulation of gene expression and transport activity is far more complex than expected.
ISSN: 0950382X
DOI: 10.1046/j.1365-2958.1998.00915.x

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