Sequence determination and modeling of structural motifs for the smallest monomeric aminoacyl-tRNA synthetase.

@article{Hou1991SequenceDA,
  title={Sequence determination and modeling of structural motifs for the smallest monomeric aminoacyl-tRNA synthetase.},
  author={Ya-Ming Hou and Kiyotaka Shiba and C Mottes and Paul R. Schimmel},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1991},
  volume={88 3},
  pages={976-80}
}
Polypeptide chains of 19 previously studied Escherichia coli aminoacyl-tRNA synthetases are as large as 951 amino acids and, depending on the enzyme, have quaternary structures of alpha, alpha 2, alpha 2 beta 2, and alpha 4. These enzymes have been organized into two classes which are defined by sequence motifs that are associated with specific three-dimensional structures. We isolated, cloned, and sequenced the previously uncharacterized gene for E. coli cysteine-tRNA synthetase (EC 6.1.1.16… CONTINUE READING

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