A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å

@article{Cusack1990ASC,
  title={A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å},
  author={Stephen Cusack and Carmen Berthet-Colominas and Michael H{\"a}rtlein and Nicolas Nassar and R. Leberman},
  journal={Nature},
  year={1990},
  volume={347},
  pages={249-255}
}
The three-dimensional crystal structure of seryl-transfer RNA synthetase from Escherichia coli, refined at 2.5 Å resolution, is described. It has an N-terminal domain that forms an antiparallel α helical coiled-coil, stretching 60 Å out into the solvent and stabilized by interhelical hydrophobic interactions and an active-site α – β domain based around a seven-stranded antiparallel β sheet. Unlike the three other known synthetase structures, the enzyme contains no classical nucleotide-binding… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 107 extracted citations

Similar Papers

Loading similar papers…