Crystal structure of the GTP-binding protein Obg from Thermus thermophilus HB8.

@article{KukimotoNiino2004CrystalSO,
  title={Crystal structure of the GTP-binding protein Obg from Thermus thermophilus HB8.},
  author={Mutsuko Kukimoto-Niino and Kazutaka Murayama and Mio Inoue and Takaho Terada and Jeremy R. H. Tame and Seiki Kuramitsu and Mikako Shirouzu and Shigeyuki Yokoyama},
  journal={Journal of molecular biology},
  year={2004},
  volume={337 3},
  pages={761-70}
}
Obg comprises a unique family of high-molecular mass GTPases conserved from bacteria to eukaryotes. Bacterial Obg is essential for cellular growth, sporulation, and differentiation. Here, we report the crystal structure of the full-length form of Obg from Thermus thermophilus HB8 at 2.07 A resolution, in the nucleotide-free state. It reveals a three-domain arrangement, composed of the N-terminal domain, the guanine nucleotide-binding domain (G domain), and the C-terminal domain. The N-terminal… CONTINUE READING

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