Article
DNA-binding of phenylalanyl-tRNA synthetase is accompanied by loop formation of the double-stranded DNA.
Journal of molecular biology - 19 Jan 2001
Dou X, Limmer S, Kreutzer R
Abstract excerpt
The phenylalanyl-tRNA synthetase (FRS) from Thermus thermophilus has previously been shown to bind DNA. We demonstrate that the "winged" helix-turn-helix motifs in the duplicate domains B5 are the relevant structural elements for this DNA-binding property. By altering particular amino acids in the "wing", the affinity of the FRS to DNA was significantly reduced. Based on experimental data, which indicate that the...
Topics
- Acylation
- Amino Acid Sequence
- Amino Acid Substitution
- Binding Sites
- DNA
- DNA-Binding Proteins
- Deoxyribonuclease I
- Helix-Turn-Helix Motifs
- Humans
- Kinetics
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Nucleic Acid Conformation
- Phenylalanine-tRNA Ligase
- Protein Binding
- Protein Conformation
- Protein Structure, Tertiary