NOVEL STEREOSPECIFICITY OF THE L-ARABINOSE-BINDING PROTEIN

被引：254

作者：

QUIOCHO, FA

VYAS, NK

机构：

来源：

NATURE | 1984年 / 310卷 / 5976期

关键词：

D O I：

10.1038/310381a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Tertiary structure refinement at 1.7 .ANG. resolution of the liganded form of L-arabinose-binding protein from Escherichia coli revealed a novel binding site geometry which accommodates .alpha.- and .beta.-anomers of L-arabinose. This detailed structure analysis provides new understanding of protein-sugar interaction, the process by which the binding protein minimizes the difference in the stability of the 2 bound sugar anomers and the roles of periplasmic binding proteins in active transport.

引用

页码：381 / 386

页数：6

共 36 条

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