X-ray structure of Escherichia coli pyridoxine 5'-phosphate oxidase complexed with FMN at 1.8 A resolution.
Safo, M.K., Mathews, I., Musayev, F.N., di Salvo, M.L., Thiel, D.J., Abraham, D.J., Schirch, V.(2000) Structure 8: 751-762
- PubMed: 10903950 
- DOI: https://doi.org/10.1016/s0969-2126(00)00162-3
- Primary Citation of Related Structures:  
1DNL - PubMed Abstract: 
Escherichia coli pyridoxine 5'-phosphate oxidase (PNPOx) catalyzes the terminal step in the biosynthesis of pyridoxal 5'-phosphate (PLP), a cofactor used by many enzymes involved in amino acid metabolism. The enzyme oxidizes either the 4'-hydroxyl group of pyridoxine 5'-phosphate (PNP) or the 4'-primary amine of pyridoxamine 5'-phosphate (PMP) to an aldehyde. PNPOx is a homodimeric enzyme with one flavin mononucleotide (FMN) molecule non-covalently bound to each subunit. A high degree of sequence homology among the 15 known members of the PNPOx family suggests that all members of this group have similar three-dimensional folds.
Organizational Affiliation: 
Institute for Structural Biology and Drug Discovery, Virginia Commonwealth University, Richmond, VA 23219, USA. msafo@hsc.vcu.edu