Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a novel ATP and riboflavin-binding fold.

@article{Bauer2003CrystalSO,
  title={Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a novel ATP and riboflavin-binding fold.},
  author={Stefanie Bauer and Kristina Kemter and Adelbert Bacher and Robert Huber and Markus Fischer and Stefan Steinbacher},
  journal={Journal of molecular biology},
  year={2003},
  volume={326 5},
  pages={1463-73}
}
The essential redox cofactors riboflavin monophosphate (FMN) and flavin adenine dinucleotide (FAD) are synthesised from their precursor, riboflavin, in sequential reactions by the metal-dependent riboflavin kinase and FAD synthetase. Here, we describe the 1.6A crystal structure of the Schizosaccharomyces pombe riboflavin kinase. The enzyme represents a novel family of phosphoryl transferring enzymes. It is a monomer comprising a central beta-barrel clasped on one side by two C-terminal helices… CONTINUE READING

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