PMID:7959032
| Citation |
Youderian, P and Arvidson, DN (1994) Direct recognition of the trp operator by the trp holorepressor--a review. Gene 150:1-8 |
|---|---|
| Abstract |
Two different X-ray co-crystal structures of the Escherichia coli trp holorepressor complexed with DNA suggest that the TrpR protein recognizes specific DNA sequences primarily with a network of water-mediated H-bonds. However, the more recent nuclear magnetic resonance (NMR) solution structures of the holorepressor-operator complex show no long-lived, ordered water molecules at the protein-DNA interface and place amino acids in intimate contact with nucleotide bases. Both genetic and biochemical studies support a model in which the trp repressor recognizes specific DNA sequences by a direct mechanism, as seen in the NMR solution structures, not by the 'indirect readout' mechanism initially proposed on the basis of X-ray studies. |
| Links | |
| Keywords |
Bacterial Proteins; Base Sequence; DNA, Bacterial/chemistry; DNA, Bacterial/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Molecular Sequence Data; Nucleic Acid Conformation; Operator Regions, Genetic; Protein Conformation; Repressor Proteins/chemistry; Repressor Proteins/metabolism; Tryptophan |
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