Crystal structure of rat biliverdin reductase |
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Authors: | Kikuchi A Park S Y Miyatake H Sun D Sato M Yoshida T Shiro Y |
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Affiliation: | RIKEN Harima Institute/SPring-8, Sayo, Hyogo 679-5148, Japan. kikuchi@spring8.or.jp |
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Abstract: | 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. |
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