Site-directed mutagenesis of loop L3 of sucrose porin ScrY leads to changes in substrate selectivity

DC FieldValueLanguage
dc.contributor.authorUlmke, C
dc.contributor.authorKreth, J
dc.contributor.authorLengeler, JW
dc.contributor.authorWelte, W
dc.contributor.authorSchmid, K
dc.date.accessioned2021-12-23T16:09:04Z-
dc.date.available2021-12-23T16:09:04Z-
dc.date.issued1999
dc.identifier.issn00219193
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/8598-
dc.description.abstractThe difference in substrate selectivity of the maltodextrin (LamB) and sucrose (ScrY) porins is attributed mainly to differences in loop L3, which is supposed to constrict the lumen of the pores. We show that even a single mutation (D201Y) in loop L3 leads to a narrowing of the substrate range of ScrY to that resembling LamB. In addition, we removed the putative N-terminal coiled-coil structure of ScrY and studied the effect of this deletion on sucrose transport.
dc.language.isoen
dc.publisherAMER SOC MICROBIOLOGY
dc.relation.ispartofJOURNAL OF BACTERIOLOGY
dc.subjectCHANNEL
dc.subjectCLONING
dc.subjectESCHERICHIA-COLI
dc.subjectGENE
dc.subjectMALTOPORIN
dc.subjectMETABOLISM
dc.subjectMicrobiology
dc.subjectOUTER-MEMBRANE
dc.subjectSTRUCTURAL BASIS
dc.subjectSUGAR TRANSLOCATION
dc.subjectTRANSPORT
dc.titleSite-directed mutagenesis of loop L3 of sucrose porin ScrY leads to changes in substrate selectivity
dc.typejournal article
dc.identifier.doi10.1128/JB.181.6.1920-1923.1999
dc.identifier.isiISI:000079146700029
dc.description.volume181
dc.description.issue6
dc.description.startpage1920
dc.description.endpage1923
dc.contributor.orcid0000-0002-8599-8310
dc.contributor.researcheridH-4472-2011
dc.contributor.researcheridAAU-7833-2021
dc.identifier.eissn10985530
dc.publisher.place1752 N ST NW, WASHINGTON, DC 20036-2904 USA
dcterms.isPartOf.abbreviationJ. Bacteriol.
dcterms.oaStatusBronze, Green Published
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