STRUCTURAL HOMOLOGY BETWEEN RBS REPRESSOR AND RIBOSE BINDING-PROTEIN IMPLIES FUNCTIONAL SIMILARITY

被引：32

作者：

MAUZY, CA ^{[1
]}

HERMODSON, MA ^{[1
]}

机构：

[1] PURDUE UNIV,DEPT BIOCHEM,W LAFAYETTE,IN 47907

来源：

PROTEIN SCIENCE | 1992年 / 1卷 / 07期

关键词：

BINDING PROTEINS; CHEMOTAXIS; ESCHERICHIA-COLI; EVOLUTION; PROTEIN HOMOLOGY; REPRESSORS; RIBOSE TRANSPORT;

D O I：

10.1002/pro.5560010702

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The deduced amino acid sequence of the rbs repressor, RbsR, of Escherichia coli is homologous over its C-terminal 272 residues to the entire sequence of the periplasmic ribose binding protein. RbsR is also homologous to a family of bacterial repressor proteins including LacI. This implies that the structure of the repressor consists of a two-domain binding protein portion attached to a DNA-binding domain having the four-helix structure of the LacI headpiece. The implications of these relationships to the mechanism of this class of repressors are discussed.

引用

页码：843 / 849

页数：7

共 42 条

[11] MISSENSE MUTATION IN THE LACI GENE OF ESCHERICHIA-COLI - INFERENCES ON THE STRUCTURE OF THE REPRESSOR PROTEIN [J].