Article
Conformational changes of the Tet repressor induced by tetracycline trapping.
Journal of molecular biology - 5 Jun 1998
Orth P, Cordes F, Schnappinger D, Hillen W, Saenger W, Hinrichs W
Abstract excerpt
The X-ray crystal structure analysis of inducer-free Tet repressor, TetR, at 2.4 A resolution identifies one of two openings of the tunnel-like binding site as the entrance for the inducer tetracycline-Mg2+, [Mg Tc]+. Recognition and binding of the inducer unleashes conformational changes leading...
Topics
- Amino Acid Sequence
- Bacterial Proteins
- Binding Sites
- Crystallography, X-Ray
- Escherichia coli
- Gene Expression Regulation, Bacterial
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Protein Conformation
- Protein Structure, Secondary
- Recombinant Fusion Proteins
- Repressor Proteins
- Tetracycline
- Water