Crystal structure of rat biliverdin reductase

被引：63

作者：

Kikuchi, A ^{[1
]}

Park, SY

Miyatake, H

Sun, DY

Sato, M

Yoshida, T

Shiro, Y

机构：

[1] RIKEN, Harima Inst, SPring 8, Sayo, Hyogo 6795148, Japan

[2] Yamagata Univ, Sch Med, Cent Lab Res & Educ, Yamagata 9909585, Japan

来源：

NATURE STRUCTURAL BIOLOGY | 2001年 / 8卷 / 03期

关键词：

D O I：

10.1038/84955

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Angstrom 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.

引用

页码：221 / 225

页数：5

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