Mutational analysis of a leucine heptad repeat motif in a class I aminoacyl-tRNA synthetase.

@article{Ohannesian1996MutationalAO,
  title={Mutational analysis of a leucine heptad repeat motif in a class I aminoacyl-tRNA synthetase.},
  author={David W. Ohannesian and Jongmin Oh and Ya-Ming Hou},
  journal={Biochemistry},
  year={1996},
  volume={35 45},
  pages={
          14405-12
        }
}
Aminoacyl-tRNA synthetases activate amino acids with ATP to form aminoacyl adenylates as the essential intermediates for aminoacylation of their cognate tRNAs. The class I Escherichia coli cysteine tRNA synthetase contains an N-terminal nucleotide binding fold that provides the catalytic site of adenylate synthesis. The C-terminal domain of the cysteine enzyme is predominantly alpha-helical and contains a leucine heptad repeat motif. We show here that specific substitutions of leucines in the… CONTINUE READING