Crystal structure of the cytochrome P-450CAM active site mutant Thr252Ala.

  title={Crystal structure of the cytochrome P-450CAM active site mutant Thr252Ala.},
  author={Reetta Raag and Susan A. Martinis and Stephen G Sligar and Thomas L Poulos},
  volume={30 48},
The crystal structure of a cytochrome P-450CAM site-directed mutant in which the active site Thr252 has been replaced with an Ala (Thr252Ala) has been refined to an R factor of 0.18 at 2.2 A. According to sequence alignments (Nelson & Strobel, 1989), Thr252 is highly conserved among P-450 enzymes. The crystallographic structure of ferrous camphor- and carbon monoxide-bound P-450CAM (Raag & Poulos, 1989b) suggests that Thr252 is a key active site residue, forming part of the dioxygen-binding… CONTINUE READING

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