Crystal structure of the intact archaeal translation initiation factor 2 demonstrates very high conformational flexibility in the alpha- and beta-subunits.

@article{Stolboushkina2008CrystalSO,
  title={Crystal structure of the intact archaeal translation initiation factor 2 demonstrates very high conformational flexibility in the alpha- and beta-subunits.},
  author={Elena A. Stolboushkina and Stanislav Nikonov and Alexei Nikulin and Udo Blaesi and Dietmar J Manstein and Roman Fedorov and Maria Garber and Oleg Nikonov},
  journal={Journal of molecular biology},
  year={2008},
  volume={382 3},
  pages={
          680-91
        }
}
In Eukarya and Archaea, translation initiation factor 2 (eIF2/aIF2), which contains three subunits (alpha, beta, and gamma), is pivotal for binding of charged initiator tRNA to the small ribosomal subunit. The crystal structure of the full-sized heterotrimeric aIF2 from Sulfolobus solfataricus in the nucleotide-free form has been determined at 2.8-A resolution. Superposition of four molecules in the asymmetric unit of the crystal and the comparison of the obtained structures with the known… CONTINUE READING
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