Article
The three-dimensional structure of trp repressor.
Nature - 1 Jan 2000
Schevitz R W, Otwinowski Z, Joachimiak A, Lawson C L, Sigler P B
Abstract excerpt
The crystal structure of the Escherichia coli trp repressor has been solved to atomic resolution. The dimeric protein has a remarkable subunit interface in which five of each subunit's six helices are interlinked. The binding of L-tryptophan activates the aporepressor indirectly by fixing the orientation of the second helix of the helix-turn-helix motif and by moulding the details of the repressor's structure...
Topics
- Bacterial Proteins
- Binding Sites
- Chemical Phenomena
- Chemistry
- Crystallization
- DNA, Bacterial
- Escherichia coli
- Macromolecular Substances
- Models, Molecular
- Mutation
- Operator Regions, Genetic