Idiosyncratic helix-turn-helix motif in Methanosarcina barkeri seryl-tRNA synthetase has a critical architectural role.

@article{Bilokapic2009IdiosyncraticHM,
  title={Idiosyncratic helix-turn-helix motif in Methanosarcina barkeri seryl-tRNA synthetase has a critical architectural role.},
  author={Silvija Bilokapic and Nives Ivi{\'c} and Vlatka Godini{\'c}-Mikul{\vc}i{\'c} and Ivo Piantanida and Nenad Ban and Ivana Weygand-Dura{\vs}evi{\'c}},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 16},
  pages={
          10706-13
        }
}
All seryl-tRNA synthetases (SerRSs) are functional homodimers with a C-terminal active site domain typical for class II aminoacyl-tRNA synthetases and an N-terminal domain involved in tRNA binding. The recently solved three-dimensional structure of Methanosarcina barkeri SerRS revealed the idiosyncratic features of methanogenic-type SerRSs; that is, an active site zinc ion, a unique tRNA binding domain, and an insertion of approximately 30 residues in the catalytic domain, which adopt a helix… CONTINUE READING
BETA

Similar Papers

Loading similar papers…