1gcu
From Proteopedia
CRYSTAL STRUCTURE OF RAT BILIVERDIN REDUCTASE AT 1.4 A
Structural highlights
FunctionBIEA_RAT Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBiliverdin 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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