Article
Seryl-tRNA synthetase from Escherichia coli: functional evidence for cross-dimer tRNA binding during aminoacylation.
Nucleic acids research - 11 Apr 1995
Vincent C, Borel F, Willison J C, Leberman R, Härtlein M
Abstract excerpt
Escherichia coli seryl-tRNA synthetase (SerRS) is a homo-dimeric class II aminoacyl-tRNA synthetase. Each subunit is composed of two distinct domains: the N-terminal domain is a 60 A long, arm-like coiled coil structure built up of two antiparallel alpha-helices, whereas the C-terminal domain, the catalytic core, is an alpha-beta structure overlying a seven-stranded antiparallel beta-sheet. Deletion of the...
Topics
- Acylation
- Amination
- Amino Acid Sequence
- Base Sequence
- Binding Sites
- DNA Primers
- DNA, Bacterial
- Escherichia coli
- Kinetics
- Molecular Sequence Data
- Mutagenesis, Site-Directed