Crystal structure of rat biliverdin reductase.
Biliverdin reductase (BVR) is a soluble cytoplasmic enzyme that catalyzes the conversion of biliverdin to bilirubin using NADH or NADPH as electron donor. Bilirubin is a significant biological antioxidant, but it is also neurotoxic and the cause of kernicterus. In this study, we have determined the crystal structure of rat BVR at 1.4 A resolution. The structure contains two domains: an N-terminal domain characteristic of a dinucleotide binding fold (Rossmann fold) and a C-terminal domain that is predominantly an antiparallel six-stranded beta-sheet. Based on this structure, we propose modes of binding for NAD(P)H and biliverdin, and a possible mechanism for the enzyme.
RIKEN Harima Institute/SPring-8, Sayo, Hyogo 679-5148, Japan. kikuchi@spring8.or.jp
A
A
Kikuchi
S Y
SY
Park
H
H
Miyatake
D
D
Sun
M
M
Sato
T
T
Yoshida
Y
Y
Shiro
D000595:Amino Acid Sequence; D000818:Animals; D001664:Biliverdine / Q000378:metabolism; D001665:Binding Sites; D018360:Crystallography, X-Ray; D006418:Heme / Q000378:metabolism; D007700:Kinetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D010088:Oxidoreductases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D044925:Oxidoreductases Acting on CH-CH Group Donors; D017434:Protein Structure, Tertiary; D051381:Rats; D016415:Sequence Alignment; D015032:Zinc / Q000032:analysis
D009243:NAD; D006418:Heme; D009249:NADP; D010088:Oxidoreductases; D044925:Oxidoreductases Acting on CH-CH Group Donors; C019789:biliverdin reductase; D015032:Zinc; D001664:Biliverdine