Allosteric interaction of nucleotides and tRNA(ala) with E. coli alanyl-tRNA synthetase.

@article{Dignam2011AllostericIO,
  title={Allosteric interaction of nucleotides and tRNA(ala) with E. coli alanyl-tRNA synthetase.},
  author={John David Dignam and Jingshu Guo and Wendell P Griffith and Nichola C Garbett and Amanda Holloway and Timothy C. Mueser},
  journal={Biochemistry},
  year={2011},
  volume={50 45},
  pages={9886-900}
}
Alanyl-tRNA synthetase, a dimeric class 2 aminoacyl-tRNA synthetase, activates glycine and serine at significant rates. An editing activity hydrolyzes Gly-tRNA(ala) and Ser-tRNA(ala) to ensure fidelity of aminoacylation. Analytical ultracentrifugation demonstrates that the enzyme is predominately a dimer in solution. ATP binding to full length enzyme (ARS875) and to an N-terminal construct (ARS461) is endothermic (ΔH = 3-4 kcal mol(-1)) with stoichiometries of 1:1 for ARS461 and 2:1 for full… CONTINUE READING