Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102.

@article{Senda1996ThreedimensionalSO,
  title={Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102.},
  author={Toshiya Senda and Katsumi Sugiyama and Hirotaka Narita and Takahiko Yamamoto and Kazuhide Kimbara and Masao Fukuda and Mamoru Sato and Kazuyoshi Yano and Yukio Mitsui},
  journal={Journal of molecular biology},
  year={1996},
  volume={255 5},
  pages={735-52}
}
The crystal structure of an enzyme having polychlorinated-biphenyl degrading activity, the BphC enzyme from Pseudomonas sp. strain KKS102, has been solved as a free form at 1.8 A resolution. This is the first three-dimensional structure among the extradiol-type dioxygenases. Based on 34,387 reflections (10.0 to 1.8 A, completeness 87.8%), a current R-factor of 20.4% (with a free R-factor of 24.3%) was obtained with a model obeying standard geometry within 0.011 A in bond lengths and 1.91… CONTINUE READING
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