Crystal structure of the unliganded alkaline protease from Pseudomonas aeruginosa IFO3080 and its conformational changes on ligand binding.

@article{Miyatake1995CrystalSO,
  title={Crystal structure of the unliganded alkaline protease from Pseudomonas aeruginosa IFO3080 and its conformational changes on ligand binding.},
  author={Haruka Miyatake and Yasuo Hata and Takahiro Fujii and Kensaku Hamada and Kazuyuki Morihara and Yukiteru Katsube},
  journal={Journal of biochemistry},
  year={1995},
  volume={118 3},
  pages={474-9}
}
The crystal structure of the unliganded alkaline protease from Pseudomonas aeruginosa IFO3080 has been determined at 2.0 A resolution by the X-ray method. The enzyme consists of N-terminal catalytic and C-terminal beta-helix domains. On structural comparison between the present unliganded enzyme and structurally- known liganded enzyme, some structural changes were observed around the active site. In the unliganded enzyme, Y216 serves as the fifth ligand for the active site zinc ion. On ligand… CONTINUE READING

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