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

被引：19

作者：

Ulmke, C

Kreth, J

Lengeler, JW

Welte, W

Schmid, K ^{[1
]}

机构：

[1] Univ Osnabruck, Fachbereich Biol Chem, AG Genet, D-49069 Osnabruck, Germany

[2] Univ Konstanz, Fak Biol, D-78457 Constance, Germany

来源：

JOURNAL OF BACTERIOLOGY | 1999年 / 181卷 / 06期

关键词：

D O I：

10.1128/JB.181.6.1920-1923.1999

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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.

引用

页码：1920 / 1923

页数：4

共 49 条

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[35] Comment on: Role of changes in the L3 loop of the active site in the evolution of enzymatic activity of VIM-type metallo-β-lactamases
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