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 language||English (US)|
|Number of pages||4|
|Journal||Journal of bacteriology|
|State||Published - Mar 1 1999|
ASJC Scopus subject areas
- Molecular Biology