PMID:1304370

Citation	Mauzy, CA and Hermodson, MA (1992) Structural homology between rbs repressor and ribose binding protein implies functional similarity. Protein Sci. 1:843-9
Abstract	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.
Links	PubMed PMC2142147 Online version:10.1002/pro.5560010702
Keywords	Amino Acid Sequence; Bacterial Proteins; Biological Evolution; Carrier Proteins/chemistry; Carrier Proteins/genetics; Carrier Proteins/metabolism; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/genetics; DNA-Binding Proteins/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Models, Molecular; Molecular Sequence Data; Periplasmic Binding Proteins; Protein Structure, Secondary; Repressor Proteins/chemistry; Repressor Proteins/genetics; Repressor Proteins/metabolism; Ribose/metabolism; Sequence Homology, Amino Acid; Structure-Activity Relationship
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