Modeling of the bacterial luciferase-flavin mononucleotide complex combining flexible docking with structure-activity data.

@article{Lin2001ModelingOT,
  title={Modeling of the bacterial luciferase-flavin mononucleotide complex combining flexible docking with structure-activity data.},
  author={Leo Yen-Cheng Lin and Traian Sulea and R. B. Szittner and V. R. Vassilyev and Enrico O. Purisima and Edward A. Meighen},
  journal={Protein science : a publication of the Protein Society},
  year={2001},
  volume={10 8},
  pages={
          1563-71
        }
}
Although the crystal structure of Vibrio harveyi luciferase has been elucidated, the binding sites for the flavin mononucleotide and fatty aldehyde substrates are still unknown. The determined location of the phosphate-binding site close to Arg 107 on the alpha subunit of luciferase is supported here by point mutagenesis. This information, together with previous structure-activity data for the length of the linker connecting the phosphate group to the isoalloxazine ring represent important… CONTINUE READING
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