PMID:8735275
| Citation |
Phillips, SE and Stockley, PG (1996) Structure and function of Escherichia coli met repressor: similarities and contrasts with trp repressor. Philos. Trans. R. Soc. Lond., B, Biol. Sci. 351:527-35 |
|---|---|
| Abstract |
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. |
| Links |
PubMed Online version:10.1098/rstb.1996.0051 |
| Keywords |
Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Base Sequence; Consensus Sequence; Crystallography, X-Ray; DNA, Bacterial/chemistry; DNA, Bacterial/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Methionine/biosynthesis; Models, Structural; Molecular Sequence Data; Nucleic Acid Conformation; Protein Structure, Secondary; Repressor Proteins/chemistry; Repressor Proteins/metabolism; Sequence Homology, Nucleic Acid; Software; Transcription, Genetic; Tryptophan/biosynthesis |
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