1GCU

CRYSTAL STRUCTURE OF RAT BILIVERDIN REDUCTASE AT 1.4 A

1GCU の概要

• エントリーDOI: 10.2210/pdb1gcu/pdb
• 分子名称: BILIVERDIN REDUCTASE A (2 entities in total)
• 機能のキーワード: biliverdin, rossmann fold, oxidoreductase
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cytoplasm: P46844
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33611.54

構造登録者

Kikuchi, A.,Park, S.Y.,Shiro, Y. (登録日: 2000-08-08, 公開日: 2001-02-08, 最終更新日: 2023-12-27)

主引用文献

Kikuchi, A.,Park, S.Y.,Miyatake, H.,Sun, D.,Sato, M.,Yoshida, T.,Shiro, Y.
Crystal structure of rat biliverdin reductase.
Nat.Struct.Biol., 8:221-225, 2001

PubMed 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.

PubMed: 11224565
DOI: 10.1038/84955

実験手法

X-RAY DIFFRACTION (1.4 Å)