1gcu

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Image:1gcu.jpg

1gcu, resolution 1.4Å

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CRYSTAL STRUCTURE OF RAT BILIVERDIN REDUCTASE AT 1.4 A

Overview

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.

About this Structure

1GCU is a Single protein structure of sequence from Rattus norvegicus. Active as Biliverdin reductase, with EC number 1.3.1.24 Full crystallographic information is available from OCA.

Reference

Crystal structure of rat biliverdin reductase., Kikuchi A, Park SY, Miyatake H, Sun D, Sato M, Yoshida T, Shiro Y, Nat Struct Biol. 2001 Mar;8(3):221-5. PMID:11224565

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