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

Christine Ulmke, Jens Kreth, Joseph W. Lengeler, Wolfram Welte, Kurt Schmid

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

The 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.

Original languageEnglish (US)
Pages (from-to)1920-1923
Number of pages4
JournalJournal of Bacteriology
Volume181
Issue number6
StatePublished - Mar 1 1999
Externally publishedYes

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Porins
Site-Directed Mutagenesis
Sucrose
Mutation
maltodextrin

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

Site-directed mutagenesis of loop L3 of sucrose porin ScrY leads to changes in substrate selectivity. / Ulmke, Christine; Kreth, Jens; Lengeler, Joseph W.; Welte, Wolfram; Schmid, Kurt.

In: Journal of Bacteriology, Vol. 181, No. 6, 01.03.1999, p. 1920-1923.

Research output: Contribution to journalArticle

Ulmke, Christine ; Kreth, Jens ; Lengeler, Joseph W. ; Welte, Wolfram ; Schmid, Kurt. / Site-directed mutagenesis of loop L3 of sucrose porin ScrY leads to changes in substrate selectivity. In: Journal of Bacteriology. 1999 ; Vol. 181, No. 6. pp. 1920-1923.
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