Common active site architecture and binding strategy of four phenylpropanoid P450s from Arabidopsis thaliana as revealed by molecular modeling.

@article{Rupasinghe2003CommonAS,
  title={Common active site architecture and binding strategy of four phenylpropanoid P450s from Arabidopsis thaliana as revealed by molecular modeling.},
  author={Sanjeewa G. Rupasinghe and Jerome Baudry and Mary A. Schuler},
  journal={Protein engineering},
  year={2003},
  volume={16 10},
  pages={721-31}
}
Despite extensive primary sequence diversity, crystal structures of several bacterial cytochrome P450 monooxygenases (P450s) and a single eukaryotic P450 indicate that these enzymes share a structural core of alpha-helices and beta-sheets and vary in the loop regions contacting individual substrates. To determine the extent to which individual structural features are conserved among divergent P450s existing in a single biosynthetic pathway, we have modeled the structures of four highly… CONTINUE READING

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