1GCU

CRYSTAL STRUCTURE OF RAT BILIVERDIN REDUCTASE AT 1.4 A

Summary for 1GCU

• Entry DOI: 10.2210/pdb1gcu/pdb
• Descriptor: BILIVERDIN REDUCTASE A (2 entities in total)
• Functional Keywords: biliverdin, rossmann fold, oxidoreductase
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasm: P46844
• Total number of polymer chains: 1
• Total formula weight: 33611.54

Authors

Kikuchi, A.,Park, S.Y.,Shiro, Y. (deposition date: 2000-08-08, release date: 2001-02-08, Last modification date: 2023-12-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.4 Å)