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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Structure and function of Escherichia coli met repressor: similarities and contrasts with trp repressor.

Transcription of genes encoding enzymes for the biosynthesis of methionine and trytophan in Escherichia coli is regulated by the ligand-activated met and trp repressors. X-ray crystallographic studies show how these two small proteins, although similar in size and function, have totally different three-dimensional structures and specifically recognize their respective DNA operator sequences in different ways. A common feature is that both repressors bind as cooperative arrays to tandem repeats of 8 base-pair 'Met' or 'Trp boxes' respectively, and the consensus sequences share the rare tetranucleotide CTAG. A series of structural and functional studies have shown how the two repressors discriminate between their operators, using a combination of direct contacts between side chains and bases, and indirect sensing of conformational properties of the DNA.[1]

References

  1. Structure and function of Escherichia coli met repressor: similarities and contrasts with trp repressor. Phillips, S.E., Stockley, P.G. Philos. Trans. R. Soc. Lond., B, Biol. Sci. (1996) [Pubmed]
 
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