The ABC maltose transporter

DC FieldValueLanguage
dc.contributor.authorEhrmann, M
dc.contributor.authorEhrle, R
dc.contributor.authorHofmann, E
dc.contributor.authorBoos, W
dc.contributor.authorSchlosser, A
dc.date.accessioned2021-12-23T16:11:19Z-
dc.date.available2021-12-23T16:11:19Z-
dc.date.issued1998
dc.identifier.issn0950382X
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/9638-
dc.description.abstractBacterial 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.
dc.language.isoen
dc.publisherBLACKWELL SCIENCE LTD
dc.relation.ispartofMOLECULAR MICROBIOLOGY
dc.subjectACTIVE-TRANSPORT
dc.subjectBINDING CASSETTE TRANSPORTER
dc.subjectBiochemistry & Molecular Biology
dc.subjectESCHERICHIA-COLI K-12
dc.subjectGENETIC-ANALYSIS
dc.subjectINNER MEMBRANE-PROTEIN
dc.subjectMALK SUBUNIT
dc.subjectMicrobiology
dc.subjectNUCLEOTIDE-SEQUENCE
dc.subjectPROTEIN-DEPENDENT TRANSPORT
dc.subjectSALMONELLA-TYPHIMURIUM
dc.subjectSTREPTOMYCES-COELICOLOR A3(2)
dc.titleThe ABC maltose transporter
dc.typereview
dc.identifier.doi10.1046/j.1365-2958.1998.00915.x
dc.identifier.isiISI:000075450900003
dc.description.volume29
dc.description.issue3
dc.description.startpage685
dc.description.endpage694
dc.contributor.orcid0000-0002-1927-260X
dc.contributor.orcid0000-0003-4874-372X
dc.contributor.researcheridA-7307-2012
dc.publisher.placeP O BOX 88, OSNEY MEAD, OXFORD OX2 0NE, OXON, ENGLAND
dcterms.isPartOf.abbreviationMol. Microbiol.
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