Structural homology between rbs repressor and ribose binding protein implies functional similarity. |
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Authors: | C A Mauzy M A Hermodson |
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Institution: | Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907. |
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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. |
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Keywords: | binding proteins chemotaxis Escherichia coli evolution protein homology repressors ribose transport |
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