title: Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli.
abstract: Flavin reductases use flavins as substrates and are distinct from flavoenzymes which have tightly bound flavins. The reduced flavin can serve to reduce ferric complexes and iron proteins. In Escherichia coli, reactivation of ribonucleotide reductase is achieved by reduced flavins produced by flavin reductase. The crystal structure of E. coli flavin reductase reveals that the enzyme structure is similar to the structures of the ferredoxin reductase family of flavoproteins despite very low sequence similarities. The main difference between flavin reductase and structurally related flavoproteins is that there is no binding site for the AMP moiety of FAD. The direction of the helix in the flavin binding domain, corresponding to the phosphate binding helix in the flavoproteins, is also slightly different and less suitable for phosphate binding. Interactions for flavin substrates are instead provided by a hydrophobic isoalloxazine binding site that also contains a serine and a threonine, which form hydrogen bonds to the isoalloxazine of bound riboflavin in a substrate complex.
authors.affiliation: Department of Molecular Biology, Swedish University of Agricultural Sciences, Biomedical Center, Uppsala.
authors.forename: M
authors.initials: M
authors.lastname: Ingelman
authors.forename: S
authors.initials: S
authors.lastname: Ramaswamy
authors.forename: V
authors.initials: V
authors.lastname: Nivière
authors.forename: M
authors.initials: M
authors.lastname: Fontecave
authors.forename: H
authors.initials: H
authors.lastname: Eklund
mesh_terms: D000249:Adenosine Monophosphate / Q000737:chemistry / Q000378:metabolism; D000595:Amino Acid Sequence; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D019143:Evolution, Molecular; D038181:FMN Reductase; D005287:Ferredoxin-NADP Reductase / Q000737:chemistry / Q000378:metabolism; D005486:Flavin Mononucleotide / Q000737:chemistry / Q000378:metabolism; D005182:Flavin-Adenine Dinucleotide / Q000737:chemistry / Q000378:metabolism; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D009249:NADP / Q000737:chemistry / Q000378:metabolism; D010710:Phosphates / Q000737:chemistry / Q000378:metabolism; D012256:Riboflavin / Q000737:chemistry / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D010710:Phosphates; D005182:Flavin-Adenine Dinucleotide; D000249:Adenosine Monophosphate; D009249:NADP; D005486:Flavin Mononucleotide; D005287:Ferredoxin-NADP Reductase; D038181:FMN Reductase; D009247:NADH, NADPH Oxidoreductases; D012256:Riboflavin