Ligand binding-induced conformational changes in riboflavin kinase: structural basis for the ordered mechanism.

@article{Karthikeyan2003LigandBC,
  title={Ligand binding-induced conformational changes in riboflavin kinase: structural basis for the ordered mechanism.},
  author={Subramanian Karthikeyan and Qingxian Zhou and Andrei L. Osterman and Hong Zhang},
  journal={Biochemistry},
  year={2003},
  volume={42 43},
  pages={12532-8}
}
Riboflavin kinase (RFK) is an essential enzyme catalyzing the phosphorylation of riboflavin (vitamin B(2)) in the presence of ATP and Mg(2+) to form the active cofactor FMN, which can be further converted to FAD. Previously, the crystal structures of RFKs from human and Schizosaccharomyces pombe have been determined in the apo form and in complex with MgADP. These structures revealed that RFK adopts a novel kinase fold and utilizes a unique nucleotide binding site. The structures of the flavin… CONTINUE READING